期刊
TOXICON
卷 101, 期 -, 页码 79-84出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2015.05.006
关键词
Antimicrobial peptides; Alpha-helix; Amphipathic; Hemolysis
资金
- Rhodes College startup funds [DOC144 (Fund112072)]
- Faculty Development Endowment summer grants [DOC731 (Fund112366)]
Two analogs of the natural peptide BmKn1 and four of BmKn2 found in the venom of the scorpion Buthus martensii Marsh have been synthesized and tested to compare their antimicrobial and hemolytic activity with the natural ones. Modifications of the natural sequence were done on the hydrophobic side of the alpha helix by increasing the size and hydrophobicity of the residues with alanine (BmKn2A1), valine (BmKn2V1) and leucine (BmKn2L1) respectively, and on the hydrophilic side by increasing the charge from +2 to +3 with two lysines (BmKn2K7). In order to study observed peptide aggregation, two peptides with one (BmKn1-6Lys) and two (BmKn1L2K2) positive charges respectively in the hydrophobic side have been also designed. Results show that the valine substituted analog BmKn2V1 and lysine substituted analog BmKn2K7 have in general, the highest antibiotic and hemolytic activity of the group. Introduction of one positive charge on the hydrophobic side shows a significant increase in antibacterial activity compared with the original sequence except for Bacillus and Enterobacter where, unexpectedly, the activity fiats-off. In contrast, the analog with two positive charges has minimal antibacterial or hemolytic activity. (C) 2015 Elsevier Ltd. All rights reserved.
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