Authors Reichelt, S. ; Eichhorn, K.-J. ; Aulich, D. ; Hinrichs, K. ; Jain, N. ; Appelhans, D. ; Voit, B.
Title Functionalization of solid surfaces with hyperbranched polyesters to control protein adsorption
Date 05.03.2009
Number 17362
Abstract Thin films of hyperbranched polyesters were studied in dry state and in aqueous buffer solution regarding their swelling behaviour and protein adsorption potential. The influence of the degree of branching, the backbone structure, flexibility as well as the polarity was varied. By changing the backbone structure from aromatic, aromatic–aliphatic to aliphatic the surface properties can be controlled from protein active to protein repelling. The higher adsorption potential observed in comparison to linear polyesters is the result of the large amount of end groups allowing the formation of hydrogen bonds, and the larger swellability of the more flexible linear polymers. The protein adsorption process was studied intensively by in-situ spectroscopic ellipsometry. Different approaches towards a proper optical model for the vis-ellipsometry data evaluation for the determination of the correct layer thickness and refractive index are discussed. IR-ellipsometric measurements using a new in-situ cell gave the full chemical evidence for the formation of thin protein adsorption layer on the polymer films in the aqueous buffer environment.
Publisher Colloids and Surfaces B: Biointerfaces
Citation Colloids and Surfaces B: Biointerfaces 69 (2009) 169-177
Tags hyperbranched polyesters protein adsorption in-situ ellipsometry swelling sensor application thin-films spectroscopic ellipsometry aromatic polyesters optical-properties liquid interfaces serum-albumin hbp-oh layers polymers water

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