Competitive adsorption of albumin against collagen at solution-air and solution-polyethylene interfaces.

The adsorption of human serum albumin (HSA) from the binary mixtures with collagen was monitored at solution-air and solution-polyethylene interfaces by the in situ measurements. The results clearly demonstrate that on both interfaces albumin is the only adsorbing protein within a large collagen solution concentration range. At the albumin concentration equal to 0.005 mg/mL, the presence of collagen in solution results in the enhancement of albumin adsorption at solution-air interface relative to its adsorption from the single protein system. The same phenomenon is manifested at the solution-polyethylene interface, although the increase in albumin adsorption at this interface occurs at the albumin concentration equal to 0.01 mg/mL. These results are attributed to the lowering in the solution-air and solution-polyethylene interfacial tensions, and thus to the increase in the spreading characteristics of albumin in the presence of collagen molecules. The desorption experiments carried out with a buffer solution on polyethylene surfaces reveal the irreversibility of adsorbed albumin from both the single and the binary mixtures with collagen. When after 20 h of adsorption from the solutions containing albumin only, collagen was added to these solutions or when the samples after that period of time were first rinsed with a buffer and then with a collagen solution, the amounts of albumin remaining at the surfaces were in both cases reduced by one-half.