AI Article Synopsis
- Bactrocerin-1, a novel antimicrobial peptide extracted from the Bactrocera dorsalis insect, consists of 20 amino acids and has a molecular weight of 2,325.95 Da, showing strong similarity to a fragment of Coleoptericin A.
- This peptide is characterized as hydrophobic and positively charged, with rich concentrations of lysine, isoleucine, and glycine, exhibiting broad-spectrum antimicrobial activity against various bacteria and fungi.
- Importantly, Bactrocerin-1 demonstrates no hemolytic activity against mouse red blood cells even at high concentrations, and its structure suggests the presence of an amphipathic alpha-helix
Article Abstract
A novel antimicrobial peptide, Bactrocerin-1, was purified and characterized from an immunized dipteran insect, Bactrocera dorsalis. Bactrocerin-1 has 20 amino acid residues with a mass of 2,325.95 Da. The amino acid sequence of Bactrocerin-1 showed very high similarity to the active fragment (46V-65S-NH(2)) of Coleoptericin A. The composition of amino acid residues revealed that Bactrocerin-1 is a hydrophobic, positively charged, and Lys/Ile/Gly-rich peptide. Minimal growth inhibition concentration (MIC) measurements for synthesized Bactrocerin-1 showed a very broad spectrum of anti-microbial activity against Gram-positive bacteria, Gram-negative bacteria, and fungi. Bactrocerin-1 did not show hemolytic activity toward mouse red blood cells even at a concentration of 50 microM. Analysis of the Helical-wheel projection and the CD spectrum suggested that Bactrocerin-1 contains the amphipathic alpha-helix.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/arch.20308 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!