IR spectral changes of bovine serum albumin upon surface adsorption.

The adsorption of bovine serum albumin from flowing solutions onto germanium and three polyetherurethanes varying in soft segment content was studied by a Fourier transform infrared/attenuated total reflectance technique. Spectral differences observed in the amide I, II, and III regions upon adsorption to all four surfaces were consistent with a loss of helix and gain of beta-structure. There appeared to be a slight difference between BSA adsorbed to germanium and the PEUs, but no distinction could be made between BSA adsorbed to the different PEUs.

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