The Effect of the Glycine Pair Motifs(Gly-Gly)on the Stability and Flexibility of Collagen
10.13865/j.cnki.cjbmb.2025.02.1456
- VernacularTitle:成对甘氨酸基序(Gly-Gly)对胶原蛋白稳定性及柔性的影响
- Author:
Xuan-Ting WANG
1
;
Meng ZHANG
1
;
Fei XU
1
Author Information
1. 江南大学生物工程学院工业生物技术教育部重点实验室,江苏无锡 214122
- Publication Type:Journal Article
- Keywords:
recombinant collagen;
thermal stability;
circular dichroism(CD);
molecular dynamics sim-ulation
- From:
Chinese Journal of Biochemistry and Molecular Biology
2025;41(4):541-550
- CountryChina
- Language:Chinese
-
Abstract:
Collagen is a matrix protein essential for maintaining the function of various tissues in ani-mals.There are many types of collagen in vertebrates,and the function of each type of collagen in the body is closely related to its sequence and structure.In addition to the common Gly-X-Y amino acid se-quence,there is also a special structure Gly-Gly-Y in the natural collagen.In order to explore its effect on collagen,this study constructed mutants containing Gly-Gly-Y at the levels of collagen polypeptides,long-chain collagen,and collagen polymers.The thermal stability of the mutant before and after mutation was characterized by circular dichroism scanning.At the same time,molecular dynamics simulation was used to calculate the hydrogen bonding probability and bending degree of collagen polypeptides,explai-ning the molecular mechanism of changes in collagen stability and flexibility.The results showed that the mutant containing the Gly-Gly structure would decrease the Tm value of the sample,but this effect would gradually weaken as the collagen triple helix region lengthened and the degree of protein self-assembly in-creased,and the reduced Tm values are 5 ℃,3 ℃,and 1 ℃,respectively.At the same time,the sim-ulation results show that the curvature of the polypeptide containing the Gly-Gly structure also increases to some extent,indicating that the structure near the mutation site has greater flexibility.This provides a new idea for the design of rubber materials with certain flexibility.
