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izvor podataka: crosbi

PGLa-H tandem-repeat peptides active against multidrug resistant clinical bacterial isolates (CROSBI ID 234287)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Rončević, Tomislav ; Gajski, Goran ; Ilić, Nada ; Goić-Barišić, Ivana ; Tonkić, Marija ; Zoranić, Larisa ; Simunić, Juraj ; Benincasa, Monica ; Mijaković, Marijana ; Tossi, Alessandro et al. PGLa-H tandem-repeat peptides active against multidrug resistant clinical bacterial isolates // Biochimica et biophysica acta. Biomembranes, 1859 (2017), 2; 228-237. doi: 10.1016/j.bbamem.2016.11.011

Podaci o odgovornosti

Rončević, Tomislav ; Gajski, Goran ; Ilić, Nada ; Goić-Barišić, Ivana ; Tonkić, Marija ; Zoranić, Larisa ; Simunić, Juraj ; Benincasa, Monica ; Mijaković, Marijana ; Tossi, Alessandro ; Juretić, Davor

engleski

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

Antimicrobial peptides (AMPs) are promising candidates for new antibiotic classes but often display an unacceptably high toxicity towards human cells. A naturally produced C-terminal fragment of PGLa, named PGLa-H, has been reported to have a very low haemolytic activity while maintaining a moderate antibacterial activity. A sequential tandem repeat of this fragment, diPGLa-H, was designed, as well as an analogue with a Val to Gly substitution at a key position. These peptides showed markedly improved in vitro bacteriostatic and bactericidal activity against both reference strains and multidrug resistant clinical isolates of Gram-negative and Gram-positive pathogens, with generally low toxicity for human cells as assessed by haemolysis, cell viability, and DNA damage assays. The glycine substitution analogue, kiadin, had a slightly better antibacterial activity and reduced haemolytic activity, which may correlate with an increased flexibility of its helical structure, as deduced using molecular dynamics simulations. These peptides may serve as useful lead compounds for developing anti-infective agents against resistant Gram-negative and Gram-positive species.

Antimicrobial peptides ; PGLa-H ; Clinical isolates ; Multidrug resistant ; Cyto/genotoxicity ; Bactericidal activity

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Podaci o izdanju

1859 (2)

2017.

228-237

objavljeno

0005-2736

10.1016/j.bbamem.2016.11.011

Povezanost rada

Biologija, Fizika, Interdisciplinarne prirodne znanosti

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