<mets:mets OBJID="eprint_3107" LABEL="Eprints Item" xsi:schemaLocation="http://www.loc.gov/METS/ http://www.loc.gov/standards/mets/mets.xsd http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-3.xsd" xmlns:mets="http://www.loc.gov/METS/" xmlns:mods="http://www.loc.gov/mods/v3" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"><mets:metsHdr CREATEDATE="2026-04-22T22:44:24Z"><mets:agent ROLE="CUSTODIAN" TYPE="ORGANIZATION"><mets:name>open</mets:name></mets:agent></mets:metsHdr><mets:dmdSec ID="DMD_eprint_3107_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:titleInfo><mods:title>Studies on a new antimicrobial peptide from Vibrio proteolyticus MT110</mods:title></mods:titleInfo><mods:name type="personal"><mods:namePart type="given">Himanshu</mods:namePart><mods:namePart type="family">Verma</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Kanti N.</mods:namePart><mods:namePart type="family">Mihooliya</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Jitender</mods:namePart><mods:namePart type="family">Nandal</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:name type="personal"><mods:namePart type="given">Debendra K.</mods:namePart><mods:namePart type="family">Sahoo</mods:namePart><mods:role><mods:roleTerm type="text">author</mods:roleTerm></mods:role></mods:name><mods:abstract>The marine environment is known for its vast diversity of the microbial population; however, less explored for bioactive compounds. In this study, an AMP produced by a new marine isolate, Vibrio proteolyticus MT110, showed broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria. The AMP was purified to homogeneity using ethyl acetate extraction followed by RP-HPLC, and LC-MS analysis showed its molecular weight as 980 Da. The MIC of AMP (peptide-MT110) was obtained in the 7.81-31.25 µg/mL range against different indicator strains. Peptide-MT110 showed stability of its antimicrobial activity at 15-121 °C and pH 4-10 and in the presence of various hydrolytic enzymes. The peaks at 1536 cm-1 and 1712 cm-1 wavenumbers in FTIR spectra confirmed the peptidic nature of AMP, and its amino acid analysis confirmed the presence of tyrosine and isoleucine. The antibacterial activity of peptide-MT110 is confirmed by PI assay and TEM. The optimization of peptide-MT110 production using statistical methods resulted in a 2.64-fold higher production. The physicochemical properties and stability in wide pH and temperature ranges showed the potential of peptide-MT110 for its development as a drug candidate. This is believed to be the first report on an AMP from Vibrio proteolyticus.</mods:abstract><mods:classification authority="lcc">QR Microbiology</mods:classification><mods:originInfo><mods:dateIssued encoding="iso8061">2024-02</mods:dateIssued></mods:originInfo><mods:originInfo><mods:publisher>TAYLOR AND FRANCIS</mods:publisher></mods:originInfo><mods:genre>Article</mods:genre></mets:xmlData></mets:mdWrap></mets:dmdSec><mets:amdSec ID="TMD_eprint_3107"><mets:rightsMD ID="rights_eprint_3107_mods"><mets:mdWrap MDTYPE="MODS"><mets:xmlData><mods:useAndReproduction>
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