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Processing of type I collagen gels using nonenzymatic glycation

โœ Scribed by Rani Roy; Adele Boskey; Lawrence J. Bonassar

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
287 KB
Volume
9999A
Category
Article
ISSN
1549-3296

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โœฆ Synopsis

Abstract

This study focuses on the development of a novel method of nonenzymatic glycation of fibrillar collagen gels. In contrast to previous studies in which type I collagen gels were glycated in the solid state, this study presents a method for glycation in solution. The type I collagen in solution or gels was exposed to a range of ribose concentrations from 0 to 250 m__M__. The binding of ribose to collagen was documented using Fourier transform infrared (FTIR) spectroscopy. formation of advanced glycation end products (AGEs) was quantified by fluorescence measurement. The bulk compressive modulus and viscoelastic time constant of processed gels were determined in stress relaxation studies. Both methods of glycation enhanced ribose addition and AGE formation in a doseโ€dependent manner, with glycation in the gel state being more efficient. Both methods enhanced mechanical properties similarly, with 250 m__M__ ribose treatment resulting in a 10โ€fold increase in bulk modulus. ยฉ 2009 Wiley Periodicals, Inc. J Biomed Mater Res, 2010

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