DataVXACS Biomaterials Science & EngineeringPaper
journal article·2023-08-14

Structure–Activity Relationship Study of Helix-Stabilized Antimicrobial Peptides Containing Nonproteinogenic Amino Acids

Takahito Ito, Wakana Hashimoto, Nobumichi Ohoka, Takashi Misawa, Takao Inoue, Ryuji Kawano, Yosuke Demizu

ACS Biomaterials Science & Engineering· Volume 9· Issue 8
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Source abstract

Abstract

Helical amphipathic peptides containing cationic and hydrophobic amino acid residues can possess potent antimicrobial activity against both Gram-positive and Gram-negative bacteria. In this study, several amphipathic peptides with enhanced helical structures containing nonproteinogenic amino acids were designed, and the relationships between the antimicrobial activity, hemolytic activity, and cytotoxicity were evaluated. In particular, the effect on the antimicrobial activity and cytotoxicity of the number and position of stapling structures introduced into the sequence was investigated. Peptide stp1 containing α,α-disubstituted amino acids showed potent antimicrobial activity against multidrug-resistant bacteria (MDRP, SP45, and Staphylococcus aureus ) without causing appreciable hemolytic activity or cytotoxicity. The cytotoxicity was found to be somewhat correlated to the hydrophobicity of the peptides.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Antimicrobial Peptides and Activities · Chemical Synthesis and Analysis · Supramolecular Self-Assembly in Materials

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Division of Organic Chemistry, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki, Kanagawa 210-9501, Japan

Graduate School of Medical Life Science, Yokohama City University, 1-7-29, Yokohama, Kanagawa 230-0045, Japan

Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-6 Naka-cho, Koganei, Tokyo 184-8588, Japan

Division of Molecular Target and Gene Therapy Products, National Institute of Health Sciences, 3-25-26, Tonomachi, Kawasaki, Kanagawa 210-9501, Japan

Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Division of Pharmaceutical Science of Okayama University, 1-1-1 Tsushimanaka, Kita 700-8530, Japan

Funding

Japan Agency for Medical Research and Development · Japan Society for the Promotion of Science

References (24)

Show source-provided references
1. 10.1016/S0140-6736(21)02724-010.1016/S0140-6736(21)02724-0 ↗
2. 10.1002/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M10.1002/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M ↗
3. 10.1074/jbc.273.6.371810.1074/jbc.273.6.3718 ↗
4. 10.1016/S0304-4157(98)00014-810.1016/S0304-4157(98)00014-8 ↗
5. 10.1039/C9MD00166B10.1039/C9MD00166B ↗
6. 10.1002/cplu.20200074910.1002/cplu.202000749 ↗
7. 10.1021/ja000563a10.1021/ja000563a ↗
8. 10.1021/ma00014a00610.1021/ma00014a006 ↗
9. 10.1021/acs.jmedchem.9b0107810.1021/acs.jmedchem.9b01078 ↗
10. 10.1038/srep0199510.1038/srep01995 ↗
11. 10.1039/C8AN00243F10.1039/C8AN00243F ↗
12. 10.1021/acsabm.8b0083510.1021/acsabm.8b00835 ↗
13. 10.1021/acsomega.9b0103310.1021/acsomega.9b01033 ↗
14. 10.3390/mi1402037310.3390/mi14020373 ↗
15. 10.3389/fmicb.2014.0018010.3389/fmicb.2014.00180 ↗
16. 10.1111/j.1747-0285.2011.01086.x10.1111/j.1747-0285.2011.01086.x ↗
17. 10.1039/D1CB00231G10.1039/D1CB00231G ↗
18. 10.3390/toxins1312086710.3390/toxins13120867 ↗
19. 10.1038/s41587-019-0222-z10.1038/s41587-019-0222-z ↗
20. 10.1002/bip.2041710.1002/bip.20417 ↗
21. 10.1007/s00726-012-1283-110.1007/s00726-012-1283-1 ↗
22. 10.1016/j.bmcl.2015.06.05310.1016/j.bmcl.2015.06.053 ↗
23. 10.1002/bkcs.1083910.1002/bkcs.10839 ↗
24. 10.1002/cbic.20170035210.1002/cbic.201700352 ↗