PGLa-H tandem-repeat peptides active against multidrug resistant clinical bacterial isolates

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• 作者：Tomislav Rončević^a ; Goran Gajski^b ; Nada Ilić^a ; Ivana Goić-Bari&scaron ; ić^c ; Marija Tonkić^c ; Larisa Zoranić^a ; Juraj Simunić^a ; ¹ ; Monica Benincasa^d ; Marijana Mijaković^a ; Alessandro Tossi^d ; Davor Juretić^a ; ^e ; ^{davor.juretic@gmail.com}
• 关键词：AO ; Acridine orange ; EtBr ; ethidium bromide ; DLPC ; 1 ; 2-dilauroyl-sn-glycero-3-phosphocholine ; diC12 ; DMSO ; dimethyl sulphoxide ; dPG ; diphosphatidylglycerol ; EDTA ; ethylenediaminetetraacetic acid ; ESBL ; extended-spectrum β-lactamase ; FBS ; foetal bovine serum ; HPBLs ; human peripheral blood leukocytes ; LUVs ; large unilamellar vesicles ; LMP ; low melting point ; MTT ; 3-(4 ; 5-dimethylthiazol-2-Yl)-2 ; 5-diphenyltetrazolium bromide ; NMP ; normal melting point ; PG ; phosphatidylglycerol ; PI ; propidium iodide
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1859
• 期：2
• 页码：228-237
• 全文大小：762 K
• 卷排序：1859

文摘

PGLa-H is one of the smallest natural antimicrobial peptides but is poorly active. Doubling its size in a tandem repeat enhanced peptide activity. A rationally guided point mutation (Val15 → Gly) improved peptide selectivity. Cytotoxicity and genotoxicity towards host blood cells were low for both peptides. Peptides were bactericidal for multidrug resistant clinical isolates.