{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T04:16:33Z","timestamp":1793333793356,"version":"4.5.0"},"reference-count":35,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,12,14]],"date-time":"2018-12-14T00:00:00Z","timestamp":1544745600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Highly acidic peptides with no disulfide bridges are widely present in the scorpion venoms; however, none of them has been functionally characterized so far. Here, we cloned the full-length cDNA of a short-chain highly acidic peptide (referred to as HAP-1) from a cDNA library made from the venom glands of the Chinese scorpion Mesobuthus martensii Karsch. HAP-1 contains 19 amino acid residues with a predicted IP value of 4.25. Acidic amino residues account for 33.3% of the total residues in the molecule of HAP-1. HAP-1 shows 76\u201398% identities to some scorpion venom peptides that have not yet been functionally characterized. Secondary structure prediction showed that HAP-1 contains a beta-sheet region (residues 9\u201317), and two coiled coil regions (residues 1\u20138 and 18\u201319) located at the N-terminal and C-terminal regions of the peptide, respectively. Antimicrobial assay showed that HAP-1 does not have any effect on the growth of the bacterium Staphylococcus aureus AB94004. However, it potently inhibits the antimicrobial activity of a 13-mer peptide from M. martensii Karsch against Staphylococcus aureus AB94004. This finding is the first characterization of the function of such highly acidic peptides from scorpions.<\/jats:p>","DOI":"10.3390\/molecules23123314","type":"journal-article","created":{"date-parts":[[2018,12,14]],"date-time":"2018-12-14T04:44:42Z","timestamp":1544762682000},"page":"3314","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the Scorpion Mesobuthus martensii Karsch"],"prefix":"10.3390","volume":"23","author":[{"given":"Wanxia","family":"Shi","sequence":"first","affiliation":[{"name":"State Key Laboratory of Biogeology and Environmental Geology &amp; School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pengchen","family":"He","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biogeology and Environmental Geology &amp; School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2675-2596","authenticated-orcid":false,"given":"Xian-Chun","family":"Zeng","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biogeology and Environmental Geology &amp; School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weiwei","family":"Wu","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biogeology and Environmental Geology &amp; School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaoming","family":"Chen","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biogeology and Environmental Geology &amp; School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,12,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1093\/nar\/gkm832","article-title":"ATDB: A uni-database platform for animal toxins","volume":"36","author":"He","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1002\/pmic.201100409","article-title":"Molecular diversity of the telson and venom components from Pandinus cavimanus (Scorpionidae Latreille 1802): Transcriptome, venomics and function","volume":"12","author":"Peigneur","year":"2012","journal-title":"Proteomics"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1862","DOI":"10.1021\/bi201633j","article-title":"Solution structure of kurtoxin: A gating modifier selective for Cav3 voltage-gated Ca2+ channels","volume":"51","author":"Lee","year":"2012","journal-title":"Biochem. 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