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Molecular design, structural analysis and bactericidal activity of derivatives of antimicrobial peptide buforin II / 药学学报
Acta Pharmaceutica Sinica ; (12): 366-371, 2013.
Article in Chinese | WPRIM | ID: wpr-235658
Responsible library: WPRO
ABSTRACT
A novel peptide, named BF2-X, was designed based on the structure-activity analysis of an analogue of Buforin II, named BF2-A. The BF2-X was a hybrid peptide containing the N-terminal residues 5 to 13 of BF2-A and three repeats of the C-terminal regular alpha-helical motif RLLR, and the residues 8 valine were replaced by leucine. The results of bioinformatics analysis had showed that compared with BF2-A, the helicity, positive charge, hydrophobicity rate and C-terminal amphipathy of BF2-X had remarkably enhanced. Both peptides showed a random coil structure in an aqueous solution, while displaying a typical alpha-helical structure in 50% trifluoroethanol solution (a membrane mimic condition). BF2-X exhibited higher alpha-helical contents than BF2-A in hydrophobic environment. BF2-X displayed potent antimicrobial activities against a broad spectrum of microorganisms. And BF2-X showed stronger antimicrobial activities against bacteria tested than parent peptide BF2-A. These results suggest that the alpha-helical content was directly correlated with the enhanced antibacterial activity. Both peptides had no hemolytic action on mouse erythrocyte.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Pharmacology / Structure-Activity Relationship / Bacteria / Proteins / Chemistry / Amino Acid Sequence / Circular Dichroism / Protein Structure, Secondary / Antimicrobial Cationic Peptides / Hydrophobic and Hydrophilic Interactions Language: Chinese Journal: Acta Pharmaceutica Sinica Year: 2013 Type: Article
Full text: Available Index: WPRIM (Western Pacific) Main subject: Pharmacology / Structure-Activity Relationship / Bacteria / Proteins / Chemistry / Amino Acid Sequence / Circular Dichroism / Protein Structure, Secondary / Antimicrobial Cationic Peptides / Hydrophobic and Hydrophilic Interactions Language: Chinese Journal: Acta Pharmaceutica Sinica Year: 2013 Type: Article