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Updated: Jun 11, 2025
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
Insight into the structure-activity relationship of thermal hysteresis activity of cod collagen peptides through
Jiajian Liang1, Xiujuan Chen1, Julieth Joram Majura1
1Shenzhen Institute of Guangdong Ocean University, Shenzhen 518108, China; College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China.
Abstract:
To elucidate the correlation between variations in thermal hysteresis activity (THA) and the physicochemical properties and structure, antifreeze peptides (AFPs) of isolated fractions (CCP-1 and CCP-2) were characterized on based peptidomics and bioinformatics. The results revealed a positive correlation between the THA of cod collagen antifreeze peptide (CCAFP) and peptide chain length, isoelectric point, and hydrophobic amino acid content. Notably, the THA of CCP-1, which has higher alkaline amino acid content, was 2.60 °C at a concentration of 10 mg/mL, significantly higher than CCP (1.90 °C) and CCP-2 (2.27 °C). Glycine, proline, and valine were the vital amino acids to the formation of hydrogen bonds. Conversely, aspartic and glutamic acids at terminal regions of AFPs tended to introduce kinks in their structures. This distortion reduced binding sites for ice crystals, thereby decreasing their THA, providing a theory for understanding the physicochemical properties and structure of AFPs that influence their THA.
