Test 2 Flashcards
what is adsorption
adhesion of molecules to solid surface (no penetration)
what affects adsorption the most
hydrophobicity and surface charge
protein adsorption increases with increasing __
hydrophobicity
besides hydrophobicity and surface charge, __ can also promote protein adsorption becuause __
surface roughness can promote adsorption because proteins will become physically trapped in the valleys of the surface
what are the chemical and physical properties governing protein adsorption
chemcial Hydrophobicity Surface Charge Physical Surface Roughness Steric hinderances
rougher surfaces will have a ___ protein adsorption
more protein adsorption
besides making a surface smoother how do you physically decrease protein adsorption
add steric hinderances
how do you decrease protein adsorption using steric hinderances
add hydrophilic, highly flexible chains on the surface that will physically block the proteins from coming into contact with the surface
for steric hinderance for protein adsorption, the chains must be __ because __
the chains must be hydrophilic so they can interact with the aqueous environment
what is PEG
PEG is a large, highly flexible hydrophilic polymer that decreases protein adsorption
PEG __ __ protein binding
decreases non specific protein binding
how does PEG decrease non specific protein binding
a large volume of the surface is taken up by these bulky chains that are in constant motion. This prevents protein adsorption
PEG is an example of ___ surface property that prevent protein adsorption
steric hinderance
what are the 4 ideal surface modification techniques
(TRDS)
- Thin (to minimize effects on bulk properties)
- Resistant to delamination (want it to stay on the surface)
- Simple and robust
- discourage surface rearrangement after treatment
what are examples of covalent surface coating
Plasma treatment and self assembling monolayers (SAM)
what is plasma treatment
assembly of species in a molecularly dissociated gaseous environment
what are the possible reactions of plasma treatment
- Etching - remove stuff from the surface
- Deposition - add stuff to the surface
- Functionaliztion - covalently add molecules
what is the name of the advantages of plasma treatment
Ratner and Hoffman
What the the advantages of plasma treatment
(g clefs)
- conformal - plasma will follow shape of implant
- free of voids
- easily prepared
- good adhesion to surface
- sterile
- low leachable substances
what are disadvantages of plasma treatment
- hard to predict composition of surface that will result
- expensive
- difficult to form uniform reaction
- easily contaminated
how are SAMs different than steric hinderance
SAMs have hydrophobic regions which will stabilize the structure (steric has hydrophilic chains)
why do SAMs attach to the surface
it is thermodynamically favored for them to attach and align
because they have a hydrophobic region, SAMs are __
amphiphilic
what are the 3 groups in SAMs
- Attachment group
- Long hydrocarbon chain
- Functional Group - can be used to alter hydrophobicity
SAMs result in __ reactions
exothermic
what is the purpose of the hydrophobic regions in SAMs
they stabilize the structure
what are advantages of SAMs
- ease of formation - can control specific areas where proteins will bind
- Chemically stable
- variety of functional groups are possible
disadvantages of SAMs
need for particular chemistry to drive attachment
what is an example of a non-covalent surface coating
surface modifying agents (SMA)
what are SMA
molecules that will spontaneously rise to the surface from the bulk, thus producing a coating
Unlike, plasma treatment and SAMs, SMA is a __
pre-fabrication design
what allows SMAs to form
there is a driving force to reduce the free energy at the surface
Which material is less likely to form SMAs and why
Ceramics because there is less atomic motion in the bulk due to electroneutrality
how do SMAs form in polymers
hydrophilic particles inside the polymer will want to move to the surface when the material is placed inside an aqueous environment
what determine the effectiveness of SMAs
- difference in free energy of the surface with and without the SMA
- Molecular motility of the SMA in the bulk to actually allow it to move to the surface
- Environment surrounding the implant must be hydrophilic to allow the hydrophilic SMA to rise to the surface
what do conversion coatings do (physiochemcial surface modification)
they form a passive layer on metals
Conversion coatings can spontaneously form due to __
the porbaix diagram
what is a major concern with biological surface modification techniques
maintaining the bioactivity of the biological molecules
PEG is an example of a __ for biological coatings
a spacer arm
in covalent biological coatings, a molecule can be bound to a __
spacer arm
how does a spacer arm work for biological coatings
the spacer arm provides space between the biomolecule and the surface. this allows for greater rotational freedom and improves the activity of the biomolecule
a spacer arm is an example of a __ biological coating
covalent
give an example of a noncovalent biological coating
a positively charged surface can attract heparin (which is negatively charged)
what information does contact angle analysis provide
information about the hydrophobicity of the surface
higher contact angel = __
more hydrophobic
what is hysteresis (for contact angle analysis)
surface tension of a material can be changed before and after water is added
contact angle analysis doesn’t provide any info about __
chemical composition of the surface
explain how contact angle analysis would appear with SMAs
SMA that would move surface in body is hydrophilic – surface becomes more hydrophilic with time – contact angle decreases with time, so advancing angle is larger
what technique would you use to view the 3D surface of a material
atomic force microscopy (ATF)
ATF doesn’t provide info about __
chemical composition
what technique would you use to find the chemical composition of a surface
ATR-FTIR
protein binding on hydrophilic surfaces are __
relatively reversible
protein binding on hydrophobic surfaces are __
irreversible (protein denature on surface)
at early time points, adsorption is ___ controled
diffusion
anything that lowers __ is favorable
∆G
what is the gibbs free energy equation for protein adsorption
∆Gadsorption = ∆Gprotein +∆Gsolvent + ∆Gsurface
adsorption will be thermodynamically favorable if __
the adsorption event lowers ∆G for one or more components without raising ∆G for another component
what factors have the largest impact on protein adsorption
(drs)
- dehydration of the surface and protein
- redistribution of charged groups
- structural rearrangment of proteins
explain how dehydration of the protein and surface affects protein adsorption
water molecules become more ordered at hydrophobic surfaces
if hydrophobic areas are able to come together through adsorption, they will reduce the hydrophobic surface area that is able to come into contact with water
this will allow water to become more disordered (increase in entropy/disorder is favored)
hydrophobic amino acids will come together to minimize its interactions with water
explain how redistribution of charge affects protein adsorptoin
adsorption is preferred when the material and the surface have opposite charges
in this case, the transfer of fewest ions is required
repulsion of material and surface can be overcome by adsorption of ions from the solution to help create opposite charges
but the adsorption of ions costs energy
explain how structural rearrangement of the protein affects protein adsorption
a less stable protein will adsorb more easily since conformational rearrangement is easier
allow for optimal conformation so that hydrophobic and charged regions of the protein can be placed to fulfill the two other properties (dehydration and redistribution of charged)
amino acids are considered __ because they can act as either ___
zwitterion - they can act as either acids or bases
what are the two amino acids that play a large role in determining 2º, 3º, and 4º structure
proline and cysteine
they are both non charged
what about proline and cysteine makes them important for determining 2º, 3º, and 4º structure
proline has a ring backbone that can limit protein folding in 3D
cysteine contains sulfide (SH) which can form disulfide bonds with other cysteine residues
__ is the linear order of amino acids
primary structure
__ is a disease in the
primary structure which dictates quaternary structure
sickle cell