This study combined multispectral techniques and computational simulations to investigate the interaction mechanisms between antifreeze peptides (AFPs), ice crystals, and myofibrillar proteins (MPs). The results showed that AFP-GDQ (THA = 2.05 °C; residual peroxidase activity 84 %) and AFP-GFA (THA = 1.98 °C; residual peroxidase activity of 70 %) were identified through screening as potentially highly active AFPs. Both peptides interacted with MP, altered the secondary structure of MP, and induced fluorescence quenching. The quenching mechanism for AFP-GDQ was static, whereas AFP-GFA exhibited dynamic quenching. In addition, molecular simulations indicated that AFP-GDQ (Asp2, Gln3, Arg5, Ala8) and AFP-GFA (Phe2, Ala3, Pro5, Ser8) could bind to both ice-crystal surfaces and MP. New insights were provided to reveal the interaction mechanism of AFP as an antifreeze agent occurring after incorporation into surimi.
Unraveling the molecular interaction mechanisms of antifreeze peptides with ice crystals and myofibrillar proteins: Insights from multispectral and molecular simulation analyses.
Jiajian Liang,Zhihang Zhao,Xiujuan Chen,Mingtang Tan,Zhongqin Chen,Ming Chen,Jing Zhang,Wenhong Cao
Published 2025 in International Journal of Biological Macromolecules
ABSTRACT
PUBLICATION RECORD
- Publication year
2025
- Venue
International Journal of Biological Macromolecules
- Publication date
2025-11-01
- Fields of study
Medicine, Materials Science, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- No claims are published for this paper.
CONCEPTS
- No concepts are published for this paper.
REFERENCES
Showing 1-48 of 48 references · Page 1 of 1
CITED BY
- No citing papers are available for this paper.
Showing 0-0 of 0 citing papers · Page 1 of 1