Purification, molecular characterization, and bioinformatics analysis of putative antimicrobial peptides isolated from the haemolymph of the mulberry silkworm, Bombyx mori.

Authors

Deeya Ghosh Dastidar, Barna Chakraborty, Suman Kumar Halder, Aveek Samanta

Published in

Journal of invertebrate pathology. Pages 108767. Oct 20, 2026. Epub Oct 20, 2026.

Abstract

Antimicrobial peptides were isolated from haemolymph of non-challenged and Escherichia coli-challenged fifth-instar Bombyx mori L. larvae by solvent extraction and reverse-phase high-performance liquid chromatography on a C18 column. Selected fractions were examined by liquid chromatography-electrospray ionization-mass spectrometry, and five peptide sequences with reported molecular masses of 1999.1731-3777.1000 Da were taken forward for computational analysis. Sequence composition, hydropathy, two-dimensional chemical representation, topology, and de novo three-dimensional models were evaluated using PEPTIDE 2.0, ProtScale, PepDraw, Protter, and PEP-FOLD. The candidates differed in length, charge-related residue content, and hydrophobicity. Leucine was abundant in all five sequences. Scanning electron microscopy (SEM) validated peptide-induced bacterial morphological alterations, such as pore formation, cytoplasmic leakage, and cell lysis. Overall, B. mori-derived AMPs exhibited strong antimicrobial activity, either beating or rivalling broad-spectrum antibiotics, and provide good candidates for the development of alternative therapeutics against bacterial pathogens.

PMID:
42901317
Bibliographic data and abstract were imported from PubMed on 21 Oct 2026.

Read full publication at:
Please sign in to see all details.

Stats

1-terrible, 9-excellent. How would you rate this publication? Sign in in to submit your rating.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.