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Pregled bibliografske jedinice broj: 851711

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


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


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

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

Izvornik
Biochimica et biophysica acta. Biomembranes (0005-2736) 1859 (2017), 2; 228-237

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

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

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biologija, Interdisciplinarne prirodne znanosti



POVEZANOST RADA


Projekt / tema
HRZZ-IP-2013-11-8481 - Biofizikalni dizajn antimikrobnih peptida i inovativni molekularni deskriptori (Davor Juretic, )
HRZZ-UIP-2013-11-4514 - Formacija i destrukcija domena u vodenim otopinama (Larisa Zoranić, )

Ustanove
Institut za medicinska istraživanja i medicinu rada, Zagreb,
Institut "Ruđer Bošković", Zagreb,
Prirodoslovno-matematički fakultet, Split,
Mediteranski institut za istraživanje života

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus


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