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Open AccessCommunication

Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the Scorpion Mesobuthus martensii Karsch

State Key Laboratory of Biogeology and Environmental Geology & School of Environmental Studies, China University of Geosciences (Wuhan), Wuhan 430074, China
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Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Molecules 2018, 23(12), 3314; https://doi.org/10.3390/molecules23123314
Received: 2 June 2018 / Revised: 24 November 2018 / Accepted: 29 November 2018 / Published: 14 December 2018
(This article belongs to the Special Issue Antimicrobial Peptides and Peptidomimetics)
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Abstract

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 76–98% 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 9–17), and two coiled coil regions (residues 1–8 and 18–19) 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. View Full-Text
Keywords: venom; highly acidic peptide; scorpion; Mesobuthus martensii Karsch; antimicrobial peptide venom; highly acidic peptide; scorpion; Mesobuthus martensii Karsch; antimicrobial peptide
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Shi, W.; He, P.; Zeng, X.-C.; Wu, W.; Chen, X. Inhibitory Effect of an Acidic Peptide on the Activity of an Antimicrobial Peptide from the Scorpion Mesobuthus martensii Karsch. Molecules 2018, 23, 3314.

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