Pretražite po imenu i prezimenu autora, mentora, urednika, prevoditelja

Napredna pretraga

Pregled bibliografske jedinice broj: 935364

Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides


Rončević, Tomislav; Vukičević, Damir; Ilić, Nada; Krce, Lucija; Gajski, Goran; Tonkić, Marija; Goić-Barišić, Ivana; Zoranić, Larisa; Sonavane, Yogesh; Benincasa, Monica et al.
Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides // Journal of medicinal chemistry, 61 (2018), 7; 2924-2936 doi:10.1021/acs.jmedchem.7b01831 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 935364 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides

Autori
Rončević, Tomislav ; Vukičević, Damir ; Ilić, Nada ; Krce, Lucija ; Gajski, Goran ; Tonkić, Marija ; Goić-Barišić, Ivana ; Zoranić, Larisa ; Sonavane, Yogesh ; Benincasa, Monica ; Juretić, Davor ; Maravić, Ana ; Tossi, Alessandro

Izvornik
Journal of medicinal chemistry (0022-2623) 61 (2018), 7; 2924-2936

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

Ključne riječi
amphipathic helix ; antibiotic-resistant bacteria ; antimicrobial peptide ; molecular dynamics ; structural flexibility

Sažetak
Antimicrobial peptides often show broad- spectrum activity due to a mechanism based on bacterial membrane disruption, which also reduces development of permanent resistance, a desirable characteristic in view of the escalating multidrug resistance problem. Host cell toxicity however requires design of artificial variants of natural AMPs to increase selectivity and reduce side effects. Kiadins were designed using rules obtained from natural peptides active against E. coli and a validated computational algorithm based on a training set of such peptides, followed by rational conformational alterations. In vitro activity, tested against ESKAPE strains (ATCC and clinical isolates), revealed a varied activity spectrum and cytotoxicity that only in part correlated with conformational flexibility. Peptides with a higher proportion of Gly were generally less potent and caused less bacterial membrane alteration, as observed by flow cytometry and AFM, which correlate to structural characteristics as observed by circular dichroism spectroscopy and predicted by molecular dynamics calculations.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Biologija, Interdisciplinarne prirodne znanosti



POVEZANOST RADA


Projekti:
--IP-2013-11-8481 - Biofizikalni dizajn antimikrobnih peptida i inovativni molekularni deskriptori (BioAmpMode) (Vukičević, Damir) ( CroRIS)
HRZZ-UIP-2013-11-4514 - Formacija i destrukcija domena u vodenim otopinama (MS-FORMDES) (Zoranić, Larisa, HRZZ ) ( CroRIS)

Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb,
Prirodoslovno-matematički fakultet, Split,
Medicinski fakultet, Split,
Mediteranski institut za istraživanje života

Poveznice na cjeloviti tekst rada:

doi pubs.acs.org

Citiraj ovu publikaciju:

Rončević, Tomislav; Vukičević, Damir; Ilić, Nada; Krce, Lucija; Gajski, Goran; Tonkić, Marija; Goić-Barišić, Ivana; Zoranić, Larisa; Sonavane, Yogesh; Benincasa, Monica et al.
Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides // Journal of medicinal chemistry, 61 (2018), 7; 2924-2936 doi:10.1021/acs.jmedchem.7b01831 (međunarodna recenzija, članak, znanstveni)
Rončević, T., Vukičević, D., Ilić, N., Krce, L., Gajski, G., Tonkić, M., Goić-Barišić, I., Zoranić, L., Sonavane, Y. & Benincasa, M. (2018) Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides. Journal of medicinal chemistry, 61 (7), 2924-2936 doi:10.1021/acs.jmedchem.7b01831.
@article{article, author = {Ron\v{c}evi\'{c}, Tomislav and Vuki\v{c}evi\'{c}, Damir and Ili\'{c}, Nada and Krce, Lucija and Gajski, Goran and Tonki\'{c}, Marija and Goi\'{c}-Bari\v{s}i\'{c}, Ivana and Zorani\'{c}, Larisa and Sonavane, Yogesh and Benincasa, Monica and Jureti\'{c}, Davor and Maravi\'{c}, Ana and Tossi, Alessandro}, year = {2018}, pages = {2924-2936}, DOI = {10.1021/acs.jmedchem.7b01831}, keywords = {amphipathic helix, antibiotic-resistant bacteria, antimicrobial peptide, molecular dynamics, structural flexibility}, journal = {Journal of medicinal chemistry}, doi = {10.1021/acs.jmedchem.7b01831}, volume = {61}, number = {7}, issn = {0022-2623}, title = {Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides}, keyword = {amphipathic helix, antibiotic-resistant bacteria, antimicrobial peptide, molecular dynamics, structural flexibility} }
@article{article, author = {Ron\v{c}evi\'{c}, Tomislav and Vuki\v{c}evi\'{c}, Damir and Ili\'{c}, Nada and Krce, Lucija and Gajski, Goran and Tonki\'{c}, Marija and Goi\'{c}-Bari\v{s}i\'{c}, Ivana and Zorani\'{c}, Larisa and Sonavane, Yogesh and Benincasa, Monica and Jureti\'{c}, Davor and Maravi\'{c}, Ana and Tossi, Alessandro}, year = {2018}, pages = {2924-2936}, DOI = {10.1021/acs.jmedchem.7b01831}, keywords = {amphipathic helix, antibiotic-resistant bacteria, antimicrobial peptide, molecular dynamics, structural flexibility}, journal = {Journal of medicinal chemistry}, doi = {10.1021/acs.jmedchem.7b01831}, volume = {61}, number = {7}, issn = {0022-2623}, title = {Antibacterial Activity Affected by the Conformational Flexibility in Glycine–Lysine Based α-Helical Antimicrobial Peptides}, keyword = {amphipathic helix, antibiotic-resistant bacteria, antimicrobial peptide, molecular dynamics, structural flexibility} }

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
  • MEDLINE


Citati:





    Contrast
    Increase Font
    Decrease Font
    Dyslexic Font