Mannosylated N-Aryl Substituted 3- Hydroxypyridine-4- Ones: Synthesis, Hemagglutination Inhibitory Properties, and Molecular Modeling

Car, Željka; Hrenar, Tomica; Petrović Peroković, Vesna; Ribić, Rosana; Seničar, Mateja; Tomić, Srđanka

doi:10.1111/cbdd.12329

Pregled bibliografske jedinice broj: 640003

Mannosylated N-Aryl Substituted 3- Hydroxypyridine-4- Ones: Synthesis, Hemagglutination Inhibitory Properties, and Molecular Modeling

Car, Željka; Hrenar, Tomica; Petrović Peroković, Vesna; Ribić, Rosana; Seničar, Mateja; Tomić, Srđanka

Mannosylated N-Aryl Substituted 3- Hydroxypyridine-4- Ones: Synthesis, Hemagglutination Inhibitory Properties, and Molecular Modeling // Chemical biology & drug design, 84 (2014), 393-401 doi:10.1111/cbdd.12329 (međunarodna recenzija, članak, znanstveni)

CROSBI ID: 640003 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Mannosylated N-Aryl Substituted 3- Hydroxypyridine-4- Ones: Synthesis, Hemagglutination Inhibitory Properties, and Molecular Modeling

Autori
Car, Željka ; Hrenar, Tomica ; Petrović Peroković, Vesna ; Ribić, Rosana ; Seničar, Mateja ; Tomić, Srđanka

Izvornik
Chemical biology & drug design (1747-0277) 84 (2014); 393-401

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

Ključne riječi
Escherichia coli; FimH lectin; hemagglutination; molecular modeling; N-aryl-substituted 3-hydroxypyridine-4- ones; a-mannopyranosides

Sažetak
Structural alterations of the aglycon portions of amannosides influence their inhibitory potency toward type 1-fimbriated Escherichia coli. The aim of our work was to prepare and explore inhibitory properties of novel mannosylated N-aryl-substituted 3- hydroxypyridine-4-ones because they possess needed structural characteristics as possible FimH antagonists. Hemagglutination inhibitory tests showed that the examined 3- hydroxypyridine-4-one a-mannosides exhibited better inhibitory activity than methyl a-D- mannopyranoside used as a reference compound. Molecular modeling studies revealed the specific interactions responsible for the observed binding activities toward the mannosespecific FimH lectin. The activity depends on the substituent in p-position on the aglycon aromatic ring.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA

Projekti:
119-1191342-2959 - Spektroskopska analiza nezasićenih sustava i spojeva metala (Miljanić, Snežana, MZOS ) ( CroRIS)
119-1191344-3121 - Sinteze i enzimske transformacije biološki aktivnih spojeva (Tomić-Pisarović, Srđanka, MZOS ) ( CroRIS)

Ustanove:
Prirodoslovno-matematički fakultet, Zagreb

Profili:

Rosana Ribić (autor)