Designation, solid-phase synthesis and antimicrobial activity of Mytilin derived peptides based on Mytilin-1 from Mytilus coruscus.
- Author:
Mei LIU
1
;
Mei WU
;
Shiquan ZHOU
;
Peng GAO
;
Tao LU
;
Rixin WANG
;
Ge SHI
;
Zhi LIAO
Author Information
1. Laboratory of Marine Living and Molecular Engineering, College of Marine Science, Zhejiang Ocean University, Zhoushan 316000, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Animals;
Anti-Infective Agents;
chemical synthesis;
pharmacology;
Antimicrobial Cationic Peptides;
chemical synthesis;
chemistry;
pharmacology;
Molecular Sequence Data;
Mytilus;
chemistry
- From:
Chinese Journal of Biotechnology
2010;26(4):550-556
- CountryChina
- Language:Chinese
-
Abstract:
As a key role in mussel defense system, Mytilin is an important antibacterial peptide isolated from the mussel serum. The structural and functional researches on Mytilin showed that the fragment connecting two beta-sheets in a stable beta-hairpin structure was probably required for antimicrobial activity. To elucidate the structural features and the antimicrobial activity of this fragment, we re-designed and synthesized two peptides corresponding to the main mimic structures of Mytilin-1 from Mytilus coruscus, we named these two peptides Mytilin Derived Peptide-1 and Mytilin Derived Peptide-2, respectively. Using a liquid growth inhibition assay, we evaluated their activity towards Gram-positive, Gram-negative bacteria and fungus. The results showed that both peptides can inhibit the growth of Gram-positive, Gram-negative bacteria and fungus. Besides, these two peptides showed high stability in heat water and human serum. These works laid the foundation for further research on the molecular mechanism of Mytilin and for further exploitation of antibacterial peptides with lower molecular mass and more stable structure.
