Ahmed, Tarek, Nash, Anthony, Clark, Kristina, Ghibaudo, Marion, De Leeuw, Nora ![]() |
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Abstract
The extracellular matrix of the dermis is a complex, dynamic system with the various dermal components undergoing individual physiologic changes as we age. Age-related changes in the physical properties of collagen were investigated in particular by measuring the effect of aging, most likely due to the accumulation of advanced glycation end product (AGE) cross-links, on the nanomechanical properties of the collagen fibril using atomic force microscope nano-indentation. An age-related decrease in the Young’s modulus of the transverse fibril was observed (from 8.11 to 4.19 GPa in young to old volunteers, respectively, P<0.001). It is proposed that this is due to a change in the fibril density caused by age-related differences in water retention within the fibrils. The new collagen–water interaction mechanism was verified by electronic structure calculations, showing it to be energetically feasible.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Chemistry |
Subjects: | Q Science > QD Chemistry |
Uncontrolled Keywords: | collagen, aging, atomic force microscopy, nanomechanics, advanced glycation end products, nanotechnology |
Publisher: | Dove Medical Press |
ISSN: | 1178-2013 |
Date of First Compliant Deposit: | 21 June 2017 |
Date of Acceptance: | 14 December 2016 |
Last Modified: | 04 May 2023 14:47 |
URI: | https://orca.cardiff.ac.uk/id/eprint/101631 |
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