期刊
AMINO ACIDS
卷 43, 期 5, 页码 2047-2058出版社
SPRINGER WIEN
DOI: 10.1007/s00726-012-1283-1
关键词
Antimicrobial peptides; Stapled peptides; Analogs; Amphipathic helix; CD spectroscopy
资金
- Czech Science Foundation [203/08/0536]
- Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic [Z40550506]
The impact of inserting hydrocarbon staples into short alpha-helical antimicrobial peptides lasioglossin III and melectin (antimicrobial peptides of wild bee venom) on their biological and biophysical properties has been examined. The stapling was achieved by ring-closing olefin metathesis, either between two S-2-(4'-pentenyl) alanine residues (S (5)) incorporated at i and i + 4 positions or between R-2-(7'-octenyl) alanine (R (8)) and S (5) incorporated at the i and i + 7 positions, respectively. We prepared several lasioglossin III and melectin analogs with a single staple inserted into different positions within the peptide chains as well as analogs with double staples. The stapled peptides exhibited a remarkable increase in hemolytic activity, while their antimicrobial activities decreased. Some single stapled peptides showed a higher resistance against proteolytic degradation than native ones, while the double stapled analogs were substantially more resistant. The CD spectra of the singly stapled peptides measured in water showed only a slightly better propensity to form alpha-helical structure when compared to native peptides, whereas the doubly stapled analogs exhibited dramatically enhanced alpha-helicity.
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