Modulation of the biophysical and biochemical properties of collagen by glycation for tissue engineering applications
Journal
Acta Biomaterialia
ISSN
1742-7061
Date Issued
2023
Author(s)
Mina Vaez
Meisam Asgari
Liisa Hirvonen
Gorkem Bakir
Emilie Khattignavong
Maya Ezzo
Sebastian Aguayo
Kathleen Gough
Laurent Bozec
Type
Resource Types::text::journal::journal article
URL Institutional Repository
Cite this document
Vaez, M., Asgari, M., Hirvonen, L., Bakir, G., Khattignavong, E., Ezzo, M., Aguayo, S., Schuh, C. M., Gough, K., & Bozec, L. (2023). Modulation of the biophysical and biochemical properties of collagen by glycation for tissue engineering applications. Acta Biomaterialia, 155, 182-198. https://doi.org/10.1016/j.actbio.2022.11.033
Subjects
advanced glycation end-products
;
atomic force microscopy
;
collagen
;
crosslinking
;
glycation
;
nanomechanics
;
collagen
;
extracellular matrix
;
glycation end products, advanced
;
humans
;
maillard reaction
;
tissue engineering
;
biomechanics
;
crosslinking
;
degradation
;
elastic moduli
;
fourier transform infrared spectroscopy
;
nanotechnology
;
tissue
;
advanced glycation end product
;
clostridiopeptidase a
;
collagen
;
collagen type 1
;
glycosylated protein
;
methylglyoxal
;
advanced glycation end product
;
collagen
;
advanced glycation end products
;
atomic-force-microscopy
;
collagen fibrils
;
collagen scaffolds
;
degradation rate
;
glycation
;
meso scale
;
nano scale
;
property
;
proteolytic degradation
;
article
;
atomic force microscopy
;
attenuated total reflectance fourier transform infrared spectroscopy
;
autofluorescence
;
biophysics
;
clostridium histolyticum
;
collagen fibril
;
competitive elisa
;
controlled study
;
coronary artery dissection
;
enzymatic degradation
;
fluorescence intensity
;
fourier transform infrared spectroscopy
;
human
;
human cell
;
in vitro study
;
lipid peroxidation
;
protein degradation
;
protein glycosylation
;
skin fibroblast
;
surface area
;
tissue engineering
;
water content
;
young modulus
;
chemistry
;
extracellular matrix
;
glycation
;
metabolism
;
collagen