A non-covalent binding strategy for the stabilization of fish collagen triple helices to promote its applications

• Published in: Food hydrocolloids 2024-07, Vol.152, p.109896, Article 109896
• Main Authors: Sun, Zhening, Ge, Yihao, Cai, Xinhui, Liu, Qian, Yang, Zhiwei, Chen, Xi, Zheng, Zhaojing
• Format: Article
• Language: English
• Subjects: Collagen helix; Denaturation temperature; Fish collagen; Hsp47; Non-covalent binding
• ISSN: 0268-005X
• DOI: 10.1016/j.foodhyd.2024.109896

Collagen, with its most characteristic structural unit, the triple helix, has wide applications in pharmaceutical and cosmetic industries. However, the application of collagen is limited by its poor thermal stability, especially fish collagen. Fish collagen, despite its abundance and eco-friendly sourcing, faces challenges like low melting temperatures and mechanical fragility due to its distinct composition. In this study, the focus was on exploring strategies to enhance the stability of fish collagen for potential human applications. To address this, our research investigated a non-covalent binding strategy, by using heat shock protein 47 (Hsp47) from zebrafish and human to stabilize fish collagen. The co-application of Hsp47 dramatically improved the rates of folding and markedly increased the denaturation temperature of fish collagen from 31.7 °C to 37.7 °C, demonstrating promising outcomes for potential in vitro applications. Optical Nanoscopy Electron Microscopy (OpNS-EM) imaging demonstrates the complex formation between Hsp47 and collagen fibers, shedding light on their interaction dynamics, while cytotoxicity assays affirm the safety of the Collagen-Hsp47 complex on human keratinocytes. This pioneering methodology applies a viable approach to stabilize fish collagen, expanding its potential applications across human-related domains. [Display omitted] •The study innovatively co-supplied fish collagen with Hsp47, boosting collagen's denaturation temperature notably.•Functional assays demonstrated the enhanced properties and superior biocompatibility of the Collagen-Hsp47 complex.•Structural analysis was pivotal in capturing the complex's structure, elucidating the non-covalent bindind mechanisms.•This research could set the groundwork for repurposing fish waste and broadening the applications of fish collagen.