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Minimising chemical crosslinking for stabilising collagen in acellular bovine pericardium: mechanistic insights via structural characterisations

DOI: 10.1016/j.actbio.2022.08.057 DOI Help

Authors: Yi Zhang (Leather and Shoe Research Association of New Zealand; Victoria University of Wellington) , Wenkai Zhang (Leather and Shoe Research Association of New Zealand) , Tim Snow (Diamond Light Source) , Ying Ju (Leather and Shoe Research Association of New Zealand) , Yang Liu (Leather and Shoe Research Association of New Zealand) , Andrew J. Smith (Diamond Light Source) , Sujay Prabakar (Leather and Shoe Research Association of New Zealand)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Biomaterialia , VOL 25

State: Published (Approved)
Published: August 2022
Diamond Proposal Number(s): 25197

Open Access Open Access

Abstract: Chemically crosslinked acellular bovine pericardium (ABP) has been widely used in clinical practice as bioprostheses. To ensure its consistency and durability, crosslinkers are used in excess, with stability guided by indicators including the hydrothermal denaturation temperature, the enzymatic resistance and the degree of crosslinking. Yet, understanding of the intermolecular structure in collagen fibrils which imparts the intrinsic stability of the ABPs is lacking, and the discrepancies in the stability criteria in varied conditions are poorly explained. In this study, synchrotron small-angle X-ray scattering (SAXS) in combination with thermal and colorimetric methods are employed to investigate the changes in the structure and the stability of ABPs during crosslinking using glutaraldehyde (GA) or 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) at different concentrations. Based on the findings, a mechanism is proposed to explicate the crosslinking effects on collagen structure and the relationship between the structure and each stability indicator. At low crosslinker concentrations, the telopeptidyl-helical linkages are preferred which cause rearrangements in the intermolecular structure of collagen, and efficiently contribute to its stabilities. Excess crosslinking is revealed by a revert trend in structural changes and the plateauing of the stabilities, assigning to the helical-helical linkages and monovalent bindings. The former would improve thermal stability but not collagenase resistance, whereas the latter have negligible effects. Overall, this study provides mechanistic understanding of the chemical crosslinking of ABPs which will contribute to the future development of more efficient and economically viable strategies to produce bioprostheses.

Journal Keywords: Bovine pericardium; Chemical Crosslinking; Collagen structure; Small-angle X-ray scattering (SAXS)

Subject Areas: Materials, Biology and Bio-materials


Instruments: I22-Small angle scattering & Diffraction

Added On: 31/08/2022 09:10

Documents:
1-s2.0-S1742706122005402-main.pdf

Discipline Tags:

Biomaterials Materials Science Biophysics Life Sciences & Biotech

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)