title: Elucidation of structural and functional integration of a novel antimicrobial peptide from Antheraea mylitta.
abstract: We report here the amino acid sequence of an antimicrobial peptide of Antheraea mylitta (peptide fraction II) effectively killed urinary tract associated MDR E. coli (Dutta et al., 2016), as Gly-Gly-Gly-Gly-Gly-Gly-His-Leu-Val-Ala. The physicochemical and biological properties of this peptide were evaluated by computational analysis and its isoelectric point, grand average of hydropathicity and Boman index values were found to be 6.74, 0.42 and -1.17kcal/mol, respectively. One valid model of peptide fraction II was constructed, that contains two antiparallel β sheets with a hairpin and appeared as 'U' shaped structure. The glycine rich composition (Gly1, Gly5,Gly6and Ala10) facilitates mostly for its flexibility or dynamicity, and in its other wing, aggregation prone residues (Leu8, Val9, Ala10) triggered its auto-aggregations when contacted only with the microbial membrane. We employed simulation of peptide binding on the membrane, showed stable and deep insertion of peptide fraction II into the membrane through its hydrophobic tail (up to 3.3±1.46Å). Molecular docking study with Patchdock server revealed that this peptide could interact with the lipid aliphatic chain of 1-palmitoyl-2-oleoyl-phosphoethanolamine (POPE) bilayer and may linked to membrane distortion as we have reported earlier. Further, the studied peptide has been predicted not to exhibit any antigenicity and non-responsive to RBC membrane. These data for the first time provide new insights of an antimicrobial peptide from silkworm A. mylitta and it may serve as the template for the design of novel peptide antibiotics from this group of insect against MDR Gram-negative bacteria.
authors.affiliation: Department of Microbiology, Vidyasagar University, Midnapore, West Bengal, India.
authors.forename: Suhrid R
authors.initials: SR
authors.lastname: Dutta
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Kharagpur, West Bengal, India.
authors.forename: Samiran S
authors.initials: SS
authors.lastname: Gauri
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Kharagpur, West Bengal, India.
authors.forename: Twisa
authors.initials: T
authors.lastname: Ghosh
authors.affiliation: Department of Microbiology, Vidyasagar University, Midnapore, West Bengal, India.
authors.forename: Suman K
authors.initials: SK
authors.lastname: Halder
authors.affiliation: Department of Microbiology, Vidyasagar University, Midnapore, West Bengal, India.
authors.forename: Pradeep K
authors.initials: PK
authors.lastname: DasMohapatra
authors.affiliation: Department of Microbiology, Vidyasagar University, Midnapore, West Bengal, India. Electronic address: mondalkc@gmail.com.
authors.forename: Keshab C
authors.initials: KC
authors.lastname: Mondal
authors.affiliation: Department of Biotechnology, Indian Institute of Technology, Kharagpur, West Bengal, India.
authors.forename: Ananta K
authors.initials: AK
authors.lastname: Ghosh
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology; D006090:Gram-Negative Bacteria / Q000187:drug effects; D016905:Gram-Negative Bacterial Infections / Q000188:drug therapy; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism; D062105:Molecular Docking Simulation; D009036:Moths / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D010714:Phosphatidylethanolamines / Q000378:metabolism; D000072757:Protein Conformation, beta-Strand
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008051:Lipid Bilayers; D009842:Oligopeptides; D010714:Phosphatidylethanolamines; C057561:1-palmitoyl-2-oleoylphosphatidylethanolamine; C046274:glycyl-glycyl-glycyl-glycine
keywords: Antheraea mylitta; Antimicrobial peptide; In silico; Peptide antibiotics