Characterisation of a novel peptide, Brevinin‐1H, from the skin secretion of Amolops hainanensis and rational design of several analogues

Abstract

As drug‐resistant bacteria have become a serious health problem and have caused thousands of deaths, finding new antibiotics has become an urgent research priority. A novel antimicrobial peptide, named Brevinin‐1H, was identified in the skin secretion of Amolops hainanensis through ‘shotgun’ cloning. It has broad‐spectrum antimicrobial activity against tested micro‐organisms and has anticancer cell activity. To improve its bioactivity and decrease its cytotoxicity, two structural analogues—Brevinin‐1Ha and Brevinin‐1HY—were designed based on the secondary structure of the natural peptide. Brevinin‐1HY, in which tyrosine substituted Pro11, had similar activity to the natural peptide against Gram‐negative bacteria and cancer cells, but showed a dramatic increase in haemolytic activity and cytotoxicity at its minimum inhibitory concentration. Brevinin‐1Ha, which transferred the Rana‐box from the C‐terminal to a central position, had significantly decreased haemolytic activity, but also in antimicrobial and anticancer activity. The present data suggest that increasing the proportion of α‐helix structure in an AMP can increase its target micro‐organism bioactivity to some extent.

Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3

“…Their hemolytic potential increased with increase in peptide concentration [10] . Generally, Brevinin peptides are hemolytic in nature [19] . Brevinin 1E, an antimicrobial peptide from the Ranidae family, has also shown severe hemolysis when added to human RBC at concentrations up to 100 μg/mL [20] .…”

“…[10] Generally, Brevinin peptides are hemolytic in nature. [19] Brevinin 1E, an antimicrobial peptide from the Ranidae family, has also shown severe hemolysis when added to human RBC at concentrations up to 100 μg/mL. [20] B1CTcu3 induced 2-60 percent lysis of RBCs in a concentration-dependent manner from 0.78 to 100 μM (S4 Appendix).…”

Brevinin-2GHk, a Peptide Derived from the Skin of Fejervarya limnocharis, Inhibits Zika Virus Infection by Disrupting Viral Integrity

“…AMPs exert their activity primarily by rupturing membranes and lysing bacterial cells [28,42,43]. It is reasonable to assume that its function in the early stage of ZIKV infection is to directly inactivate the virus.…”

Modification Strategy of D-leucine Residue Addition on a Novel Peptide from Odorrana schmackeri, with Enhanced Bioactivity and In Vivo Efficacy

“…For example, the MIC of brevinin-1SPb and brevinin-1DYa against the growth of S. aureus was 13 µM and 32 µM with strong haemolysis [ 52 ]. On the other hand, by comparison with other brevinin-1 peptides, such as Ose [ 53 ], brevinin-1H [ 54 ], and B1A [ 55 ], B1OS-D-L showed comparable or even better antibacterial activity against Gram-positive bacteria with a lower level of haemolysis. Researchers have shown that the immune response of waxworms is quite similar to that of mammals [ 56 ].…”