Loughborough University
Leicestershire, UK
LE11 3TU
+44 (0)1509 263171
Loughborough University

Loughborough University Institutional Repository

Please use this identifier to cite or link to this item: https://dspace.lboro.ac.uk/2134/26830

Title: A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response
Authors: Wilson, Samantha L.
Guilbert, Marie
Sule-Suso, Josep
Torbet, James
Jeannesson, Pierre
Sockalingum, Ganesh D.
Yang, Ying
Issue Date: 2014
Publisher: © Federation of American Societies for Experimental Biology
Citation: WILSON, S. ... et al., 2014. A microscopic and macroscopic study of aging collagen on its molecular structure, mechanical properties, and cellular response. FASEB Journal, 28 (1), pp.14-25.
Abstract: During aging, collagen structure changes, detrimentally affecting tissues' biophysical and biomechanical properties due to an accumulation of advanced glycation end-products (AGEs). In this investigation, we conducted a parallel study of microscopic and macroscopic properties of different-aged collagens from newborn to 2-yr-old rats, to examine the effect of aging on fibrillogenesis, mechanical and contractile properties of reconstituted hydrogels from these collagens seeded with or without fibroblasts. In addition to fibrillogenesis of collagen under the conventional conditions, some fibrillogenesis was conducted alongside a 12-T magnetic field, and gelation rate and AGE content were measured. A nondestructive indentation technique and optical coherence tomography were used to determine the elastic modulus and dimensional changes, respectively. It was revealed that in comparison to younger specimens, older collagens exhibited higher viscosity, faster gelation rates, and a higher AGE-specific fluorescence. Exceptionally, only young collagens formed highly aligned fibrils under magnetic fields. The youngest collagen demonstrated a higher elastic modulus and contraction in comparison to the older collagen. We conclude that aging changes collagen monomer structure, which considerably affects the fibrillogenesis process, the architecture of the resulting collagen fibers and the global network, and the macroscopic properties of the formed constructs.
Description: This paper was submitted for publication in the journal FASEB Journal and the definitive published version is available at https://doi.org/10.1096/fj.13-227579
Sponsor: Funding from the Engineering and Physical Sciences Research Council (EPSRC; Swindon, UK) Doctoral Training Centre (DTC) in Regenerative Medicine (grant EP/F/500491/1), Alliance bilateral program (Egide and British Council) and the exchange program in EuroMagNET II (Grenoble, France) are gratefully acknowledged. M.G. is a recipient of a fellowship from the Région Champagne-Ardenne, France.
Version: Submitted version
DOI: 10.1096/fj.13-227579
URI: https://dspace.lboro.ac.uk/2134/26830
Publisher Link: https://doi.org/10.1096/fj.13-227579
ISSN: 0892-6638
Appears in Collections:Published Articles (Mechanical, Electrical and Manufacturing Engineering)

Files associated with this item:

File Description SizeFormat
Wilson_FASEB ORIGINAL submission_uncorrected.pdfSubmitted version1.07 MBAdobe PDFView/Open


SFX Query

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.