Title: Hydration and nanomechanical changes in collagen fibrils bearing advanced glycation end-products
Authors: Andriotis, Orestis G. 
Elsayad, Kareem 
Smart, David E 
Nalbach, Mathis 
Davies, Donna 
Thurner, Philipp J. 
Category: Original Research Article
Issue Date: 1-Apr-2019
Andriotis, O. G., Elsayad, K., Smart, D. E., Nalbach, M., Davies, D., & Thurner, P. J. (2019). Hydration and nanomechanical changes in collagen fibrils bearing advanced glycation end-products. Biomedical Optics Express, 10(4), 1841–1855. https://doi.org/10.1364/BOE.10.001841
Journal: Biomedical Optics Express 
ISSN: 2156-7085
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.
Keywords: Nanomechanics; biological tissue
DOI: 10.1364/BOE.10.001841
Organisation: E317 - Institut für Leichtbau und Struktur-Biomechanik 
License: In Copyright 1.0
Publication Type: Article
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