Proteins and Amino acids Flashcards
Describe the structural characteristics of proteins.
- Differentiated from carbohydrates and fats with the addition of nitrogen (as well as carbon hydrogen and oxygen)
- Amino acids are the basic building blocks of proteins BUT not all amino acids are protein building blocks. There are hundreds of non-protein amino acids that have other uses.
- Each amino acid contains
1. An amino group
2. A corboxylic group
3. A unique side group R which differentiates amino acids - Whilst there approximately 1000 amino acids in nature? The human body only uses 20?
- The amino acid chain is the primary structure and folds in a certain pattern to create 3-D structure which is closely linked to the function of the protein
Name the 9 essential amino acids
Clue: PVT TIM HiLL
Which of the essential amino acids is contentious and why?
Histidine
- it is synthesised in children but in adults whilst intestinal bacteria can produce histadine, it is not clear how much is provided.
- It is the only Amino acid that does not appear to impair protein synthesis when it is deficient in the diet so that seems to make it nonessential in nature.
List the main functions of protein
Growth and Maintenance
Hormones and receptors
Enzymes
Immunoglobulins (or antibodies)
Transport
Buffers
Fluid balance
Multiple functions of glycoproteins
How are proteins involved in the bodies growth and maintenance?
Proteins are the building blocks of muscles, blood, skin and most body structure.
- BONES are formed of collagen matrix (made up of amino acid) which provides a framework for minerals to deposit on.
- Ligaments, tendons, blood vessel walls, skin all use collagen as a building material
- ACTIN and MYOSIN filaments involved in muscle contractions are also protein
- Proteins are also needed for the replacement of cells. For example in the skin and the gastrointestinal tract cells are replaced every 4 to 5 days.
How are proteins involved with hormones and receptors?
Give 4 examples
Some hormones are derived from cholesterol such as reproductive hormones, cortisol, glucocorticoids for example.
Others are made from
Amino acids.
Tyrosine + Iodine»_space;> thyroid hormones
Tyrosine.»_space;> needed for the neurotransmitters dopamine, norepinephrine, epinephrine
Tryptophan»_space;> needed for the hormones/ neurotransmitters serotonin and melatonin
two polypeptide chains - insulin
one polypeptide chain - glucagon, PTH, calcitonin
Cell membrane proteins are receptors for hormones
How are proteins involved in the immune system?
Immunoglobulins are proteins found in blood and body fluids and are used by the immune system to identify and neutralise foreign materials such as bacterial viruses.
We have IgG, IgA, IgM and IgE
How is protein involved in transport systems in the body?
Give 4 examples
Some proteins act like a taxi service combining with other substances in the blood or within cells to provide a mode of transport. Without these proteins, we would not be able to deliver vital nutrients..
Eg:
Albumin - the most predominant protein in blood which can bind to calcium, zinc and B6 as well as steroids and fatty acids
Transferrins which bind to iron
ceruloplasmin which binds to copper
Haemoglobin which transports oxygen in the blood
How is protein involved in buffers?
Name 2 amino acids that buffer
This is to do with maintaining a pH of 7.35 to 7.45 in the blood. There are many mechanisms to help this and one of these are certain amino acids that have sidechain (R groups) that can easily pick up or let go of hydrogen ions thus helping to regulate acid balance in body fluids.
Proteins that have a lot of of these types of amino acids make good buffers.
Histadine is the best buffer .
Cysteine is also a buffer
What are some examples of glycoproteins?
Proteins bound to a sugar/carbohydrates,
Eg:
Mucins: found in mucus and saliva and provide protection and lubrication.
ABO blood type antigens - determines what blood group we are
Hormones: LH, FSH, T-SHIRT
Major Histocompatibility complex
proteoglycans shock absorbers that draw in fluid and keep it hydrated.
What is deamination in terms of protein metabolism?
Why does it happen?
Deamination is the removal of the nitrogen containing amino group from amino acids.
This is necessary for protein to be stored as fat or used as energy. When the protein drops nitrogen what’s left are amino acid fragments that can be used to produce glucose or ketones?
What is the byproduct of deamination and how are its potentially dangerous effects dealt with?
When the nitrogen group is removed from the amino acid, ammonia is formed which is very toxic.
It is the urea cycle that ensures it is excreted. Ammonia is converted to water soluble compounds so that it can be excreted as part of urine by the kidneys.
The Urea cycle takes place in the liver. if the liver is not functioning well it affects the urea cycle which can lead to a buildup of ammonia – hyper ammoniaemia.
Another benefit of the urea cycle is the that it is the sole endogenous source of amino acids arginine and citrulline, plus ornithine which is an important liver support and detox agent .
What is the importance of transamination?
It is very important in the synthesis of some non-essential amino acids .
When one non-essential amino acid is in good supply and another is low but in demand it is helped out by the one that is in good supply.
The amino group of an amino acid is transferred onto an enzyme. The enzyme then transfers the amino group onto a keto acid, thus forming a new amino acid.
It is a homeostatic mechanism
What is the co-factor transamination requires for a reaction to occur?
Where do we find it?
B6
Avocado
Bananas
Fish
green vegetables
lentils
Meat
pistachios
sunflower seeds
walnuts
Whole grains
What do we mean by the amino acid pool?
Why is it important to have a regular supply of protein?
- Amino acids freed from proteins when the proteins break down + amino acids from diet derived sources?
- Amino acid are utilised or excreted. They are not stored.
Essential amino acids generally have a longer half life than non-essential.
What might cause protein loss to occur?
- stress causes protein loss due catabolic actions of stress hormones such as cortisol and therefore when dealing with a stressed client they may need additional protein until the stress is dealt with
- Starvation or disease that leads to a lack of glucose and fat availability. The body will dismantle tissue proteins for energy and this will lead to tissue wasting.
What are the considerations when it comes to protein quality?
amino acid composition.
- Animal protein has all the amino acids
- Plant proteins are generally missing some and therefore in order to meet the needs for all essential amino acids you would need to combine plant sources.
digestibility
It’s all good and well to have all the amino acids but how well are they being absorbed?
- Animal protein is generally hard to digest
- Plant protein is easier to digest but
- it still has fibre which has to be got through in order to access the amino acid
- it also has anti-nutrient factors such as phytates and lectins
Quality is also determined by how the food is prepared - soaking, fermenting and sprouting improves digestibility.
Plants also contain fibre, probiotics and phytonutrients which they make make them a superior choice .
How might one optimise protein digestion?
- Chew properly so it is broken down as much as possible in the mouth.
- Eat mindfully so that the body is in a state of rest and digest.
- Consume zinc and B6 rich food which is vital for HCl production.
- Apple cider vinegar and a little water before meals.
- Better herbs 15 minutes before meals to stimulate the release of pancreatic juices.
- Betaine hydrochloride supplements to stimulate HCL
When is the fermentation of undigested protein that reaches the colon a problem?
Undigested protein which is in the colon is fermented. This can be used to produce short chain fatty acids, but it can also go down other pathways to create toxic metabolites such as ammonia to get into the bloodstream and create systemic problems.
This is more likely to happen with animal protein and when protein is combined with other foods or when too much protein is eaten.
What happens if an amino acid is missing but all the others are available to make a protein?
Which are the 4 amino acids most likely to be limiting.
The protein cannot be made.
If an essential amino acid is supplied less than the amount needed to support the protein synthesis it is called a limiting amino acid.
The amino acids in shortest supply and most likely to be limiting our lysine, threonine, methionine and tryptophan.
List six vegan foods that are complete protein
Buckwheat
Chia seeds
Hemp seeds
Pumpkin seeds
Quinoa
Tempeh
Do plant foods always need combining in one meal?
No.
The amino acid pool is stable enough to allows us to have access to amino acids throughout the day
What are the negative effects of animal proteins?
- More difficult to digest.
- Increases the acidic burden.
- The amino acid methionine is highly abundant in animal proteins and has an immune stimulating effect on T cells.
Excess methionine is associated with
- overactive immune responses – autoimmunity and chronic inflammation.
- increased homocysteine which is associated with atherosclerosis.
- And if not organic, can contain chemical residue.
- their food might contain pesticides
- oral or topical dosing of animals
What conditions/presentations are associated with long-term high intake of animal protein?
- Skeletal disease Osteoporosis: one of the ways that the body buffers the increased acidity from excessive protein, particularly animal protein is to release calcium – an alkalising mineral - from the bone
- Increased cancer risk - WHO classifies red meat as probable cause of cancer
-
Cardiovascular disease / atherosclerosis: increases oxidative stress and inflammation in the endothelium. This is problematic because when the lining is damaged, this is when arthrosclerosis becomes a risk due to the buildup of LDL ans
Foam cells
Disorders of liver function
Kidney disease - the extra acidity from high and more protein intake needs buffering by the kidneys. They are required to work hard to filter the increased urea that is generated.
Increased muscle soreness post exercise
Mitigate with alkaline rich fruit and vegetables to buffer the protein derived acid load
What are some good sources of plant based protein?
Peas
Legumes
Whole-grain
Nuts
Seeds
Vegetables - broccoli
What are some reasons to consume a high proportion of plant based protein in the diet?
Why do they have these benefits?
Think about all the things that animal based proteins can cause health problems with and Plant based proteins do the opposite…
Protective against
- cancer
- autoimmunity
- diabetes mellitus
- cardiovascular disease
Assist with healthy aging with a lower levels of acidic forming essential amino acids that can increase the expression of the enzyme TOR which regulates cell growth and when over expressed it has been shown to accelerate ageing.
Benefits are thought to be due to the presence of health supporting fibre, phytonutrients nutrients, and probiotics
How much protein do we need?
Deficiency at < 0.4 - 0.5 grams
Per kilo
General recommendation : 0.75 g per kg of the midpoint of the healthy weight range for your height and gender. (1 g for vegans to accommodate for the lower protein bioavailability)
For athletes per
Kg
- 1 g for minimal
- 1.3 g for moderate
- 1.6 g for intense
Pregnancy: add 6g per day
Lactation:
- add 11g per day 0-6 month
- add 8 g per day thereafter
Difficult to determine because there are no physiological deficiency symptoms until you get to a point of severe deficiency in which case you will find growth failure and tissue wasting. Do you like a generic symptoms because individual proteins are not able to do their job such as immunoglobulin but this could be done to all sorts of other things as well.
What groups are protein deficiency more likely to affect?
- Children with highly refined diets that are low high high-quality
- Teenagers doing the same or dieting.
- Older people who is immobility, poor chewing, digestive health and living situation reduce their intake/digestion/absorption.
- Anorexia nervosa sufferers. - vicious cycle because the very nutrients that could be used to support the production of neurotransmitters and other compounds that could bring some balance to reduce mental health issues is missing.
- Recover recovering patients from surgery or trauma
- Homeless and disadvantage people. People living in poverty and substandard condition
- Drug and alcohol addiction because the very nutrients that could be used to support the production of neurotransmitters and other compounds that could bring some balance to reduce addiction is missing.
- Those with chronic digestive conditions and using proton pump inhibitor. The lack of hydrochloric acid impaired digestion and absorption of protein.
- Chronic active infections deplete body proteins. 
What do amino acids do apart from protein building blocks for human protein tissue
- Contribute to the synthesis of hormones and neurotransmitters
- or act as neurotransmitters in their own right (e.g. glycine)
- act as methyl donors (e.g.:methionine)
- build bile acids for digestion
- Act as precursor for nitric oxide production (e.g. arginine)
- Help detoxify thousands of chemicals (i.e.: phase 2 liver pathways)
- Act as pre-cursers for the manufacturer of endogenous antioxidants (eg; glutathione which is comprised of three different amino acids)
How do you assess the amino acid status of a person and why would you do that?
You can use plasma or urine samples to explore insufficiency – imbalances
Especially useful for
- Mood - Certain aminoacids are crucial for the production of brain chemicals
- chronic fatigue syndrome due to mitochondrial inefficiency or following long-term PPI use reducing amino acid absorption
- Cardiovascular disease risk screen: high levels of amino acids Leucine, isoleucine and Valine and homocysteine linked to heart disease
Explain what a complete protein is and provide three examples of food that fit this category
A complete protein is one that has all of the nine essential amino acids.
All animal proteins have this
This is harder to achieve with non-animal proteins but examples are buckwheat, Chia/hemp/pumpkin seeds, quinoa, and Tempeh
The amino acid tyrosine is required for the formation of certain hormones - name two.
Thyroid hormones require tyrosine + iodine
Dopamine, Norepinephrine and epinephrine produce
Why can oedema occur when protein levels fall too low?
Albumin (and other proteins) draws water in. Coptic pressure. It holds water in the blood vessels. if the protein is too low, it can’t retain the water and it leaks out of the vessels into the interstitial .
Explain what happens in urea cycle
When we need to utilise protein for fuel or there is too much energy intake overall we will need to convert protein into fat for storage.
The body can’t do that while the Amine group is attached. So it goes through a process of deamination with the Amine group is removed produces ammonia which is very toxic to the body.
The ammonia therefore goes through the urea cycle word is transformed into urea which can then be safely filtered and excreted through the kidneys
What can we do to address intestinal permeability?
What illnesses can intestinal and permeability cause?
Two prong attack
A. Remove the cause
B. supply nutrients to support interacyte junctions
- Glutamine supplementation
- Glutamine which food such as cabbage juice, spirulina, asparagus, broccoli, cod, and salmon
- N-acetylene glucosamine - in shellfish to support mucosal integrity
- Quercetin
- Zinc for rapid cell division and five junction support
- Antioxidants
- herbs, particularly mucosal ones such as slippery elm and marshmallow
- Bone broth which is rich in collagen, glucosamine, chondroitin and glycine
 Intestinal permeability causes coeliac disease, IBD, candidiasis, Cibo, food allergies/intolerance, nutrient deficiencies
AMINO ACID GLUTAMINE
Is glutamine an essential, non-essential or conditionally essential amino acid and why?
It is conditionally essential. Although is the most abundant amino acid? It is also one that is widely utilised particularly in gastrointestinal health and immune function. For this reason it can get used up in times of acute stress or injury and become deficient.
!!!
AMINO ACID GLUTAMINE
What are the two main roles of glutamine?
- It is the preferred fuel for rapidly dividing cells such as enterocytes (gut support) and lymphocytes and macrophages (immunity)
- It behaves as a buffer receiving excess ammonia before releasing it needed for analysis.
AMINO ACID GLUTAMINE
List four functions and their associated therapeutic uses for glutamine
Apart supporting effective gut permeability…
- Immunity.
Support lymphocyte and macrophage proliferation and the production of cytokines by these immune cells. Used for recurrent infections and compromised immunity. - Hypoglycaemia.
Glutamine is a substrate for gluconeogenesis needed for low sugar states - Muscle recovery.
Glutamine is abundant in muscles and it can be used for fast exercise recovery and to reduce muscle breakdown - neurotransmitter.
It is converted to glutamate which is excitatory before being converted together which is inhibitory if this conversion is operating well, glutamine supplementation can have an anxiety relieving, sleep supporting effect
Note the conversion from glutamate to GABA requires vitamin B six, taurine and zinc
Delete
One to 30 g per day (ideally in the mornings to be used as soon as possible after being mixed
Don’t use with anti-seizure medications
Caution usage for cancer due to glutamine ability to fuel growth and metabolism
AMINO ACID CYSTEINE
Is cysteine an essential, a non-essential or a conditionally essential and why?
What are the three cofactors?
It is a conditionally essential amino acid so the body can make it but when it is in a particular demand then it might need to be obtained from the diet.
Dietary sources include legumes, sunflower seeds, eggs, and chicken.
Most sulphur in food is in the form of protein bound cysteine
Cofactors are B6, B9 and B12
AMINO ACID CYSTEINE
Which antioxidant is cysteine component of?
Glutathione.
Glutathione is comprised of three amino acids – cysteine, glutamic acid and glycine
It is cysteine that is the rate limiting amino acid for glutathione synthesis.
It is and therefore very important for detoxification and antioxidant support
AMINO ACID CYSTEINE
What are four functions of the therapeutic uses of cysteine and in what form is it usually supplemented?
it is usually supplemented in the form of N-Acetyl Cysteine because it is easier for the body to absorb
- Liver detoxification/antioxidant.
- It is a building block of glutathione and as such plays a crucial role in the bodies antioxidant defence
- it is the source of sulphate used in phase 2 liver detoxification pathways.
- it is crucial in drug metabolism in liver because drugs deplete Glutathione and cysteine regenerates it
… and thus is used for liver support, healthy aging support and ulcerative colitis
- Reproductive health
- helps to promote healthy sperm production
- Positively impacts serum testosterone
… and thus is used therapeutically for male infertility
- Respiratory health
- expectorant properties ie: breaks up mucus to easie elimination from the respiratory tract
… and thus is used for respiratory infections such as bronchitis, cystic fibrosis, asthma
- Insulin resistance
- increases insulin sensitivity due to antioxidant properties and reduction in oxidative stress.
… and thus is used for diabetes, Lyus and Pcos.
Also
- HIV support because the body uses up a lot of glutathione to manage this disease
- Neuro degenerative diseases - because oxidative stress is a driver
Most helpful in situations where there is a lot of mucus buildup and the mucus is hard to remove from the body
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AMINO ACID - METHIONINE
It is an essential, a non-essential or a conditionally essential amino acid?
What does it have in common Cysteine?
It is an essential amino acids and can be found in
- Beef eggs, chicken etc HIGH source
- Beans, Brazil nuts, sunflower seeds and whole-grains (e.g. quinoa
Like cysteine is it a sulphur containing amino acid.
AMINO ACID - METHIONINE
What are the functions of methionine?
Why is balance of this amino acid so important?
Whilst methionine is absolutely essential to health we don’t want too much of it.
+ve
Methionine is a major methyl donor and that’s referring to the fact that it can donate a methyl group which then allows the formation of other important compounds in the body.
For example, DNA methylation if we don’t have sufficient DNA methylation it causes instability
-ve
On the other hand, if we have too much Methylation, it can be implicated in accelerated aging and increased cancer risk.
This is because once METHIONINE donates its methyl group you are left with the compound HOMOCYSTINE which can be damaging in the body for example it can damage vascular endothelium and contribute to atherosclerosis, it has been linked with miscarriage, Alzheimer’s and osteoporosis
…So in normal circumstances, the body fairly quickly converts it back to methionine or onto cysteine where it may be converted to either tourine or all important glutathione. The big thing to remember is that those conversions are reliant on vitamin B6, B9and B12.
AMINO ACID CARNITINE
Essential, non essential or conditionally essential?
Co factors?
A non-essential amino acid that is synthesised from the essential amino acids lysine and methionine.
B3, B6 and C are cofactors
Food sources are nuts, seeds, avocado, asparagus, spinach, red meat, dairy
AMINO ACID CARNITINE
What are the functions and therapeutic uses of CARNITINE?
It helps the body to synthesise ATP from fatty acids.
So it is all about supporting the mitochondria
Skeletal muscle and cardiac muscle really rely on these fatty acids for their ATP production.
It helps to remove potentially toxic metabolites out of the mitochondria. So it preserves or maintain the health of the mitochondria.
Therapeutic uses include:
- hyperthyroidism- thyroid hormone antagonist (inhibits physiological action of the thyroid hormone)
- Weight loss by helping the body to burn fat effectively but not on its own. Once used glucose and glycogen stores through activity for energy then helping the body to burn fat.
- Heart failure. With heart failure, there was a decreased capacity to generate ATP.
- infertility - sperm count and motility and quality
- physical and mental fatigue and concentration
- athletic performance and endurance
- ADHD
Delete
- can increase blood thinning when taking anticoagulant
- contraindicated with hypothyroidism
Its use to be associated with nausea, vomiting, abdominal cramps, heartburn, gastritis, diarrhoea, body and seizure, but don’t need high doses
AMINO ACID CREATININE
Essential, non essential or conditionally essential?
Where is it found?
Non essential
Made up of the amino acids arginine , glycine and methionine.
About 95% of body creatine is found in the muscles (with some also in the brain)
AMINO ACID CREATININE
Functions
Functions as a fast source of ATP in the form of creatinine phosphate. So … it is a storage form of ATP.
It enables explosive power in the muscles for 8 to 12 seconds . For Skeletal muscle and cardiac muscle.
Not endurance. For high intensity training and muscle building.
It plays an important role in cardiovascular health . It is the first molecule to be depleted in cardiac ischaemia? It is used in those with heart failure to delay the onset of fatigue with exercise.
AMINO ACID CREATININE
Instructions and cautions with supplementation
Drugs interactions:
- High doses Might affect renal function
- neohrotic drugs may effect kidneys
Can cause abdominal pain, nausea, diarrhoea, palpitations and muscle cramping.
Hydration is important because it can cause muscles to draw water from the rest of the body
AMINO ACID GLYCINE
Essential, non essential or conditionally essential?
Where is it found?
Cofactors
Conditionally essential when there are lots of stresses on the body as used for
- haem synthesis when blood is needed
- collagen formation for growth and repair
- glycine conjugation for liver detoxification
Food sources: banana, bone broth, cabbage, cauliflower, eggs, fish, legumes, pumpkin, seaweed, spinach
Cofactors - B6 and serine
AMINO ACID GLYCINE
Functions
Collagen synthesis:
- Collagen is the most abundant protein in the body and it is made up of one third of glycine. Every third amino acid in the collagen peptide chain is glycerin.
- Collagen is crucial for structural integrity in bones, skin, GIT, tendons, and ligaments.
- Use therapeutically for GIT repair to deal with intestinal permeability mucus membrane repair , skin integrity and wound healing and muscular skeletal integrity
Liver Detox/liver support
- glycine conjugates with toxins in its own right helping clear up phase 1 toxins
- part of the tripeptide glutathione which plays a fundamental role in liberty detoxification
- support digestion due to bile acid
Inhibitory Neurotransmitter
in the central nervous system and therefore calming so
- good for insomnia
- good for cognition/memory/learning especially when induced by anxiety
AMINO ACID TAURINE
Essential, non essential or conditionally essential?
Co factors?
Conditionally essential - normally synthesises in the body in adequate amounts from Cysteine with the help of vitamin B6.
During times of extreme stress and illness the body may not be able to produce enough touring and supplementation may be needed.
Only in animal sourced food such as chicken, turkey thighs and fish
What are 5 therapeutic uses for taurine?
- Muscle health - skeletal and cardiac
- highly concentrated in muscles and play a role alongside calcium in contraction
- Heart health with its muscle supporting, anti-inflammatory, blood pressure lowering properties
- Therapeutic uses include heart failure; hypertension; atrial fibrillation (unstable heart beat) ; sarcopenia and slates down Duchenne muscular dystrophy - Antioxidant properties so protects mitochondria from ROS and is high in neutrophils has anti inflammatory and anti oxidant effects.
Used therapeutically for atherosclerosis and sperm health
- A Neuro modulator in the CNS particularly in relation to the inhibitory neurotransmitter GABA.
Supports the development of the cerebellum.
Therapeutic uses where reduce Neuro excitation is required - Parkinson’s, epilepsy, insomnia
- Bile formation.
Remember Bile is produced in the liver, stored in the gallbladder and then released into the small intestine for the digestion and absorption of fats.
Also needed for liver detox to carry away the products of detoxification.
- Insulin resistance and T2D

What are the three amino acids that make up the antioxidant glutathione.
Which is the limiting amino acid?
Glutathione is made up of three amino acids:
1. Glutamate (Glutamic Acid) 2. Cysteine 3. Glycine
Cysteine is the rate-limiting amino acid, meaning its availability is the key factor in glutathione production.
Is theanine essential, non-essential or conditionally essential?
what is the main source and food?
Essential.
Found in green tea which is why green tea which does have caffeine isn’t as stimulating as black tea
It has 20 mg in a typical cup, but a therapeutic dose is more like 50 to 200 mg
What is theanine used for therapeutically and why?
This is used to balance restlessness and anxiety and therefore helpful for
- Study/concentration
- Anxiety/agitation (including PMS)
- stress and hypertension that is related to stress
- Insomnia
- low mood
Thin is used for these conditions because it
- Increases GABA and blocks excitatory glutamate receptors
- Increases serotonin and dopamine
- Is mood enhancing
Is Tyrosine an essential, conditionally essential or non-essential amino acid?
What are its food sources?
Conditionally essential.
It is derived from
Phenylalanine and this conversion can be impaired in situations of high and ongoing stress.
Food sources are nuts, seeds, lagoons, whole grains, fish, meat, poultry
What system of the body is tyrosine used to support and why?
What hormones, neurotransmitters and other chemicals is it a precursor for?
Tyrosine supports endocrine health.
Remember, there is a precursor to thyroid hormones.
It is also a precursor to the neurotransmitters dopamine epinephrine and Nora epinephrine.
There is a precursor for melanin
What are the therapeutic uses for tyrosine?
Adrenal fatigue, which can result from excessive cortisol and adrenaline production due to high stress
Hypothyroidism
ADHD - think about tyrosines thank you because of the influence on increasing dopamine and adrenaline role with dopamine and adrenaline and the part these play in cognition, learning, memory
Depression
Anxiety
Cognition - dopamine and noradrenaline
Is Lycine an essential, conditioning essential or non-essential amino acid?
What food do we find it in?
Essential
Legumes, eggs and red meat
Why are lysine and arginine described as antagonists to each other?
Lysine decreases viral replication, which is why it is used for cold sores.
Arginine increases viral replication
What are four functions of lysine and their associated therapeutic uses?
- Decreases viral replication and therefore used for cold sores.
- Forms part of collagen and therefore used for repair of tissue and muscle, building muscle and osteoporosis. As well as anything else or collagen is involved such as skin.
- Aids intestinal absorption of calcium, iron and zinc. These nutrients are used for osteoporosis, hair loss, and anaemia.
- Glucose lowering effect which means it is used to treat hypoglycaemic and diabetes.
Is Arginine an essential, conditioning essential or non-essential amino acid?
What food do we find it in?
Conditionally essential.
Found in meat, nuts and seeds, seaweed and watermelon
What are the functions and associated therapeutic uses for Arginine
 it is a precursor to nitric oxide and therefore very important for vasodilation and lowering blood pressure.
This can be used to treat hypertension, cardiovascular disease, sports performance due to increase blood flow and erectile dysfunction
Why could using a amino acids for therapeutic purposes in the long-term lead to imbalance?
Amino acids compete with each other at the cell surface for transportation through the membrane
Using just one amino acid or a small number of amino acids, give those amino acids in advantage in terms of absorption .
Long-term, this can lead to imbalance
What groups have most isolated amino acids have not been evaluated
Pregnancy
Breastfeeding
When thinking about utilising amino acids or where there appears to be impaired utilisation of amino acids we first must think about the diet. Why?
They might be a lack of micro nutrients that are used in amino acid conversions
for example, zinc, vitamin B6 and vitamin B12.
Always try to address the diet first.
What is a free form amino acid?
by free we mean that they are non-peptide linked which means they are not peptide bonded they can be very efficiently absorbed because they are predigested in a sense.
even in the absence of stomach acid and pancreatic secretions they are absorbed.
This is where the useful in cases where you have a client with digestive issues because they can absorb the amino acids while we work on improving their digestive system
What would be an appropriate amino acid supplement and dosage for a 30-year-old woman with low mood, poor sleep, carbohydrate cravings and PMS?
Overall, this is suggesting Tryptophan because it increases melatonin (poor sleep) and serotonin (mood, PMS, carbohydrate cravings).
Dosage: 100-600 mg
Theanine might also be appropriate:
- PMS- because of Gabba’s inhibitory and calming effect reducing anxiety and agitation
- Low mood
- Sleep:
Glycine and Taurine for sleep too
What would be an appropriate amino acid supplement and dosage for a 65 kg woman with vitiligo?
The amino acid most commonly used here is phenylalanine which promotes normal melanin synthesis via the tyrosine pathway.
Dosage: 150 - 7000 mg
What would be an appropriate amino acid supplement and dosage for a 25-year-old man with recurrent cold sore outbreaks.
Lysine inhibits viral replication.
At the same time, we should be avoiding arginine rich foods because they have the opposite effect of increasing viral replication
Dosage of 300 to 3000 mg
What would be an appropriate amino acid supplement and dosage for an 18-year-old student stressed out about her exams.
So we could look at theanine because it calms the nervous system, but it doesn’t cause drowsiness but appears to promote the ability to concentrate.
Dosage range - 50-200 mg
What would be an appropriate amino acid supplement and dosage for a middle-aged man with fatigue and lack of motivation due to a stressful job.
So my suggestion would be Tyrosine because tyrosine goes on to increase production of dopamine, adrenaline and noradrenaline . The key thing we’re looking at here is the dopamine because low dopamine is quite strongly associated with lack of motivation?
Dopamine and Noradrenaline are both important for cognition and learning and memory but also for having the motivation to complete tasks.
Long-term stress can affect the adrenals and this is where Tyrosine can also be helpful.
Dose: 400-6000 mg
What would be an appropriate amino acid supplement and dosage for a 40-year-old woman with hyperthyroidism
Carnitine because it is a thyroid hormone antagonist in high doses.
Dose: 1-2 g twice a day
What would be an appropriate amino acid supplement and dosage for a 55 year-old overweight man with hypertension
Arginine because it is a vasodilator and it also tends to protect the integrity of the endothelium
Dose- 6-12 g
Taurine also helps with high blood pressure
Dose: 1500 mg per day but taken in 3 doses.
Because he is overweight, we might also consider giving him Carnitine but this needs to be combined with increased physical activity in order to use a glycogen supplies first so that fats can be transported into the cells by Carnitine for fat burning,
Dose- 1-2g a day
What are the main functions that can be restored by providing amino acids give examples of the amino acids involved?
- to assist neurotransmitter and hormone systems.
Glutamine, glycine and taurine - To restore physical and logical barriers in the gut.
Glutamine and glycine - Blood glucose stabilisation/Type II diabetes.
Glutamine, taurine, lysine, cysteine - Utilisation of fatty acids for energy.
Carnitine - Hepatic and GI detox.
Cysteine, methionine and glycine - Oxidative damage when self for amino acids are in good supply.
Methionine and cysteine
