Journal
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A
Volume 93A, Issue 3, Pages 843-851Publisher
WILEY
DOI: 10.1002/jbm.a.32231
Keywords
tissue engineering; collagen; hydrogel; scaffold; mechanical properties; FTIR
Funding
- NIAMS NIH HHS [P30 AR046121-09, P30 AR046121] Funding Source: Medline
- NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES [P30AR046121] Funding Source: NIH RePORTER
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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 mM. 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 dose-dependent manner, with glycation in the gel state being more efficient. Both methods enhanced mechanical properties similarly, with 250 mM ribose treatment resulting in a 10-fold increase in bulk modulus. (C) 2009 Wiley Periodicals, Inc. J Biomed Mater Res 93A: 843-851, 2010
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