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UT BME 352 > Exam 1 > Flashcards

Exam 1 Flashcards

1
Q

factors that are used to classify medical devices

A

invasiveness and time spent within the body

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2
Q

biomaterials

A

materials used within the body to replace or heal body tissues and/or functions

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3
Q

three classes of biomaterials

A

metals, ceramics, and polymers

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4
Q

factors that go into material choice

A

bulk property similarity, surface property similarity, processability, and FDA regulation

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5
Q

bulk properties

A

mechanical, diffusion, optical, electrical (brain, muscles, heart, etc.)

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6
Q

surface properties

A

biomaterials should be inert (chemically inactive) so as to not elicit a host response

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7
Q

processability

A

how easily can it be manufactured?

is it commercially viable to produce?

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8
Q

FDA regulation

A

tested for safety and efficacy

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9
Q

biocompatibility requirements

A

must be able to be in contact w/ living tissue without:

  • causing harmful tissue reaction that would compromise their function (pain, swelling, necrosis)
  • causing a systemic toxic reaction (immune rejection)
  • having tumorigenic potential
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10
Q

tumorigenic potential

A

difficult to show since tumor formation occurs over time

ex: flaking off of polymers in polymer-metal joints (these may be suitable for older patients since it normally takes about 10 years for negative effects)

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11
Q

type 1 diabetes

A

beta cells are destroyed and do not secrete insulin

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12
Q

potential treatment methods for diabetes using biomaterials (brainstorming)

A

insulin delivery

beta cell protection

replacement of dead beta cells

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13
Q

stent function

A

improve blood flow created by plaque

metal mesh is put around balloon and inflated in blood vessel

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14
Q

questions to ask when working with biomaterials

A

why are there different biological responses to the same materials?

how does the body respond to foreign materials?

how does the body judge between foreign and self?

how do cells see?

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15
Q

how do cells see?

A

cells “see” via proteins

proteins cause a signaling cascade that causes behavior changes in the cell

proteins are polymeric chains of amino acids

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16
Q

primary structure

A

amino acids

primary bonding types: ionic, covalent, and metallic

17
Q

secondary structure

A

alpha helix or beta sheets via molecular interactions such as: dipole-dipole, hydrogen bonds, polar molecular induced dipole, or fluctuating dipole

18
Q

tertiary strucutre

A

polypeptide chain or protein folding

19
Q

quaternary structure

A

assembled, multiprotein subunits

20
Q

protein adsorption

A

dissolved, soluble proteins in solution will deposit onto the surface of another object

creates a new “surface” and identity that can be recognized by the body

21
Q

protein adsorption spontaneity

A

favorable and irreversible process

22
Q

enthalpy

A

heat or bond energy that is present in a system

affected by charges

23
Q

entropy

A

disorderedness of a system

increases when moving from “one” to “many”

24
Q

how can enthalpy change?

A

changes in bond energy in protein due to structural changes

amount of energy between the surface and protein

amount of energy between the protein and material surface with other molecules in solution (ex: blood)

25
Q

general change in enthalpy in protein adsorption

A

enthalpy is generally positive but not as large compared to entropy

energy of bonds formed is greater than energy of bonds lost (not necessarily referring to quantity of bonds changed)

26
Q

how does the rate of protein adsorption change as the surface becomes covered?

A

rate of protein adsorption slows

initial adsorption rate on a clean surface is high

further adsorption occurs as molecules rearrange to create new free surface (ex: protein layer may go from wide and short to tall and skinny)

26
Q

how does the rate of protein adsorption change as the surface becomes covered?

A

rate of protein adsorption slows

initial adsorption rate on a clean surface is high

further adsorption occurs as molecules rearrange to create new free surface (ex: protein layer may go from wide and short to tall and skinny)

27
Q

ionic bonding

A

transfer of valence electrons

28
Q

covalent bonding

A

sharing of valence electrons

29
Q

metallic

A

delocalization of valence electrons

30
Q

why does protein adsorption lead to an increase in entropy?

A

as proteins adsorb to the surface, this frees up water molecules to move around, creating disorder/an increase in entropy

31
Q

low entropy is…

A

unfavorable

32
Q

if your surface is somewhat hydrophobic, is protein adsorption favorable?

A

yes

proteins that adsorb will “kick out” the ordered water and decrease the unfavorable water-surface interaction

33
Q

forming an ionic bond reduces…

A

enthalpy

UT BME 352 (1 decks)

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