Abstract
Abstract Protein adsorption on solid surfaces is characterized by multivalence, binding-unit overlap, sequential adsorption, surface allosterics, lateral interactions and pronounced adsorption-desorption hysteresis, giving rise to the sequential, hystallosteric, adsorption model ("SHA model"). Adsorption isotherms of fibrinogen on a titanium miniplates and of the growth factors rhBMP-2 and rhVEGF165 on PDLLA nanofiber fleeces are presented. Controversial Langmuir type isotherms of fibrinogen and rhVEGF165 can be understood on the basis of singular long-lived metastable states central to the SHA-model.
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