A novel antifungal peptide with 36 amino acids was identified by functional screening of a marine
metagenomic library. The peptide did not show similarity with any existing antimicrobial peptide sequences in the databank.
The108 bp ORF designated as mmgp1 was cloned and expressed in Escherichia coli BL21 (DE3) using pET expression
system. Mass spectrometry analysis of the purified recombinant peptide revealed a molecular mass of 5026.9 Da. The
purified recombinant peptide inhibited the growth of Candida albicans and Aspergillus niger. The peptide was predicted
to adopt α- helical conformation with an extended coil containing a ligand binding site for N-acetyl-D-glucosamine. The
α- helicity of the peptide was demonstrated by circular dichroism spectroscopy in the presence of chitin or membrane
mimicking solvent, trifluoroethanol. The chitin binding property of the peptide was also confirmed by fast performance
Keywords: Marine metagenome, gene expression, purification, antifungal peptide, fungal infections, systemic fungal, infections, human pathology, therapeutic agents, gene clusters, DNA.
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