On the effect of pepsin incubation on type I collagen from horse tendon: Fine tuning of its physico-chemical and rheological properties.
Abstract: Type I collagen is commonly recognized as the gold standard biomaterial for the manufacturing of medical devices for health-care related applications. In recent years, with the final aim of developing scaffolds with optimal bioactivity, even more studies focused on the influence of processing parameters on collagen properties, since processing can strongly affect the architecture of collagen at various length scales and, consequently, scaffolds macroscopic performances. The ability to finely tune scaffold properties in order to closely mimic the tissues' hierarchical features, preserving collagen's natural conformation, is actually of great interest. In this work, the effect of the pepsin-based extraction step on the material final properties was investigated. Thus, the physico-chemical properties of fibrillar type I collagens upon being extracted under various conditions were analyzed in depth. Correlations of collagen structure at the supramolecular scale with its microstructural properties were done, confirming the possibility of tuning rheological, viscoelastic and degradation properties of fibrillar type I collagen.
Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.
Publication Date: 2023-12-01 PubMed ID: 38043667DOI: 10.1016/j.ijbiomac.2023.128489Google Scholar: Lookup
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Summary
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This study investigates the changes to the physical-chemical and rheological properties of Type I collagen, frequently used in creating medical devices, when processed with pepsin. This examination provides in-depth analysis of the various extraction processes and their impact on the collagen’s microstructure.
Objective of the Study
- The research aims to understand the effect of pepsin—an enzyme used to extract collagen—on the physical-chemical and rheological properties of Type I collagen. The focus is on collagen derived specifically from horse tendon, often used in medical devices due to its bioactivity.
Significance of the Study
- Understanding the changes in collagen’s properties due to the extraction process influences the design process for medical devices and scaffolds. The desired physical characteristics and performance of these medical products can be precisely adjusted by fine-tuning the extraction process.
- Preserving the natural conformation of collagen while mimicking the hierarchical features of tissues is crucial in bioengineering. This research provides insights into controlling these elements.
Methods and Processes
- The study takes a comprehensive look at the physico-chemical properties of fibrillar Type I collagens under different extraction conditions, focusing on pepsin-based extraction. This enzyme is used to break down proteins and peptides into smaller fragments, or amino acids.
Results of the Study
- By varying the extraction conditions, the research acknowledges the potential to alter the rheological (flow and deformation), viscoelastic (material’s response under stress over time), and degradation properties of collagen.
- It confirms the linkage between collagen’s microstructural properties and the structure at the supramolecular scale (structure of complex, multi-molecular systems).
Cite This Article
APA
Salvatore L, Russo F, Natali ML, Rajabimashhadi Z, Bagheri S, Mele C, Lionetto F, Sannino A, Gallo N.
(2023).
On the effect of pepsin incubation on type I collagen from horse tendon: Fine tuning of its physico-chemical and rheological properties.
Int J Biol Macromol, 256(Pt 2), 128489.
https://doi.org/10.1016/j.ijbiomac.2023.128489 Publication
Researcher Affiliations
- Typeone Biomaterials Srl, Via Europa 167, Calimera, 73021 Lecce, Italy. Electronic address: l.salvatore@typeone.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: francesca.russo@unisalento.it.
- Typeone Biomaterials Srl, Via Europa 167, Calimera, 73021 Lecce, Italy. Electronic address: m.natali@unisalento.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: zahra.rajabimashhadi@unisalento.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: sonia.bagheri@unisalento.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: claudio.mele@unisalento.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: francesca.lionetto@unisalento.it.
- Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: alessandro.sannino@unisalento.it.
- Typeone Biomaterials Srl, Via Europa 167, Calimera, 73021 Lecce, Italy; Department of Engineering for Innovation, University of Salento, Via Monteroni, 73100 Lecce, Italy. Electronic address: nunzia.gallo@unisalento.it.
Conflict of Interest Statement
Declaration of competing interest The authors declare no conflict of interest.
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