Abstract
Accumulation of advanced glycation end-products (AGEs) in biological tissues occurs as a consequence of normal ageing and pathology. Most biological tissues are composed of considerable amounts of collagen, with collagen fibrils being the most abundant form. Collagen fibrils are the smallest discernible structural elements of load-bearing tissues and as such, they are of high biomechanical importance. The low turnover of collagen cause AGEs to accumulate within the collagen fibrils with normal ageing as well as in pathologies. We hypothesized that collagen fibrils bearing AGEs have altered hydration and mechanical properties. To this end, we employed atomic force and Brillouin light scattering microscopy to measure the extent of hydration as well as the transverse elastic properties of collagen fibrils treated with ribose. We find that hydration is different in collagen fibrils bearing AGEs and this is directly related to their mechanical properties. Collagen fibrils treated with ribose showed increased hydration levels and decreased transverse stiffness compared to controlled samples. Our results show that BLS and AFM yield complementary evidence on the effect of hydration on the nanomechanical properties of collagen fibrils.
Highlights
Modern diet in western societies is largely enriched in sugars causing increasing levels of obesity and diabetes
We tested the effect of sugar-mediated cross-links in collagen fibrils on their hydration and nanomechanical properties
Our results show that ribose-treated samples have a lower indentation modulus, which can be explained by their higher water content measured by Atomic force microscopy (AFM) and is consistent with Brillouin light scattering (BLS) measurements
Summary
Modern diet in western societies is largely enriched in sugars causing increasing levels of obesity and diabetes. The aldehyde or ketone group of a reducing sugar reacts with the free amino group of an amino acid. A glycated lysine can further react with a lysine or arginine forming an AGE cross-link either intra- or intermolecularly. Because collagen turnover is reduced with age [19], AGEs accumulate in healthy elderly individuals [20], such that glycation of collagen becomes more prevalent with increasing age
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