5. You are given two sets of thin samples in which one set is very hydrophobic a

Question

5. You are given two sets of thin samples in which one set is very hydrophobic and one set is very hydrophilic. Each sample is 1 cm2 in surface area. You can ignore the depth of the material How would you test if albumin adsorption to this material is dynamic or static? (4 pts) If you adsorb albumin for one minute, what is the approximate number of albumin on the surface of the material (more on hydrophobic, less on hydrophobic, or equal)? (2 pts) If you adsorb albumin for 24 hours, what is the approximate number of albumin on the surface of the material (more on hydrophobic, less on hydrophobic, or equal)? (2 pts) a. b. c. d. If you adsorb albumin for 24 hours and then expose fibrinogen to high molecular weight kininogen (HMWK) at a very low concentrated solution but has lot more affinity to the surfaces, predict and explain the likely outcome of albumin for both type of surfaces? (4 pts)

Explanation / Answer

a. albumins dynamic and static adsorption can be measured by contact angle, contact angle is less and albumin is dynamic in case of hydrophilic surface and contact angle is more in case of hydrophobic surface and albumin tend to be static. Another method is calculating sorption isotherm measurements (+ve values for hydrophilic and –ve values for hydrophobic surfaces/interactions) or by surface plasmon resonance (values on higher side for hydrophilic and liquid tend to be dynamic and lower side for hydrophobic and static )

b. Albumins are naturally hydrophilic proteins hence more albumin should be there on hydrophilic thin film and less albumin on hydrophobic thin film.

c. after 24 hours dehydration occurs and albumun becomes hydrophobic, hence should have more albumin attached to hydrophobic surface or almost equal amount like hydrophilic surface

d. after 24 hours dehydration occurs and albumun becomes hydrophobic and fibrinogen prefers hydrophobic albumin. it should attach to hydrophobic surface of albumin which is already strongly attached to hydrophobic surface (as per research fibrinogen prefers hydrophobic albumin than hydrophilic albumin). Kininogen especially high molecular weight removes fibrinogen from albumin both invitro and invivo. Upon exposure to HMWK fibrinogen will be removed (this is brought about by increasing the hydrophilicity of albumin, hence fibrinogen can no more attach to albumin). Now albumin has become more hydrophilic it cannot (less amount) sticks less to hydrophobic surface and sticks more to hydrophilic surface.

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