{
      "number": 2,
      "subjects": [
        "QR"
      ],
      "eprintid": 3107,
      "date": "2024-02",
      "userid": 2,
      "official_url": "https:\/\/www.tandfonline.com\/doi\/full\/10.1080\/10826068.2023.2209892",
      "rev_number": 5,
      "creators": [
        {
          "name": {
            "lineage": null,
            "given": "Himanshu",
            "honourific": null,
            "family": "Verma"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Kanti N.",
            "honourific": null,
            "family": "Mihooliya"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Jitender",
            "honourific": null,
            "family": "Nandal"
          }
        },
        {
          "name": {
            "lineage": null,
            "given": "Debendra K.",
            "honourific": null,
            "family": "Sahoo"
          }
        }
      ],
      "dir": "disk0\/00\/00\/31\/07",
      "keywords": "Antimicrobial peptide; MIC; Vibrio proteolyticus; amino acid analysis; response surface methodology.",
      "lastmod": "2024-06-24 02:36:17",
      "ispublished": "pub",
      "pagerange": "193-206",
      "publisher": "TAYLOR AND FRANCIS",
      "id_number": "10.1080\/10826068.2023.2209892",
      "metadata_visibility": "show",
      "date_type": "published",
      "eprint_status": "archive",
      "status_changed": "2024-06-24 02:36:17",
      "volume": 54,
      "datestamp": "2024-06-24 02:36:17",
      "uri": "http:\/\/crdd.osdd.net\/open\/id\/eprint\/3107",
      "note": "The copyright of this article belongs to TAYLOR AND FRANCIS ",
      "refereed": "TRUE",
      "contact_email": "kps@imtech.res.in",
      "publication": "PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY",
      "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.",
      "type": "article",
      "title": "Studies on a new antimicrobial peptide from Vibrio proteolyticus MT110"
    }