"The measurement of conformational stability of proteins adsorbed on si" by Magdalena Prokopowicz, Bogdan Banecki et al.
 

Title

The measurement of conformational stability of proteins adsorbed on siloxanes

Document Type

Article

Publication Date

2-1-2003

Publication Title

Journal of Biomaterials Science, Polymer Edition

Abstract

The paper investigates the conformational stability of bovine serum albumin (BSA) and fibrinogen during 24-h incubation in turn with a linear silicone polymer (polydimethylsiloxane (PDMS)), with linear silicone oligomers (hexamethyldisiloxane and octamethyltrisiloxane) and with cyclic silicone oligomers (octamethylcyclotetrasiloxane (D4) and decamethylcyclopentasiloxane (D5)). Ten-fold and 100-fold excesses of siloxanes with respect to the proteins were used. Using fluorescence spectroscopy of tryptophan located in the domain of proteins and fluorescence of 8-anilino-1-naphthalenesulfonic acid (1,8-ANS), which interacts with hydrophobic domains of proteins, changes in the tertiary structure of the protein were recorded. The results demonstrated that BSA does not change its native form during 24-h incubation with siloxanes. In contrast, the tertiary structure of fibrinogen was found to be altered by both short-chain linear siloxanes: (hexamethyldisiloxane and octamethyltrisiloxane) and long-chain PDMS. The changes can be observed only at a 100-fold excess of siloxanes with respect to the protein. No conformational changes in fibrinogen exposed to cyclic siloxanes were observed.

Volume

14

Issue

2

First Page

103

Last Page

118

DOI

https://doi.org/10.1163/156856203321142560

ISSN

0920-5063

Comments

ESSN: 1568-5624

Rights

Taylor & Francis

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