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Designation, solid-phase synthesis and antimicrobial activity of Mytilin derived peptides based on Mytilin-1 from Mytilus coruscus / 生物工程学报
Chinese Journal of Biotechnology ; (12): 550-556, 2010.
Article in Chinese | WPRIM (Western Pacific) | ID: wpr-292238
Responsible library: WPRO
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.
Subject(s)
Full text: Available Database: WPRIM (Western Pacific) Main subject: Pharmacology / Molecular Sequence Data / Chemistry / Amino Acid Sequence / Antimicrobial Cationic Peptides / Mytilus / Anti-Infective Agents Limits: Animals Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2010 Document type: Article
Full text: Available Database: WPRIM (Western Pacific) Main subject: Pharmacology / Molecular Sequence Data / Chemistry / Amino Acid Sequence / Antimicrobial Cationic Peptides / Mytilus / Anti-Infective Agents Limits: Animals Language: Chinese Journal: Chinese Journal of Biotechnology Year: 2010 Document type: Article
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