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001-es BibID:BIBFORM090862
035-os BibID:(WoS)000622919300001 (Scopus)85099773383
Első szerző:Izsépi László
Cím:Bacterial Cell Wall Analogue Peptides Control the Oligomeric States and Activity of the Glycopeptide Antibiotic Eremomycin : solution NMR and Antimicrobial Studies / László Izsépi, Réka Erdei, Anna N. Tevyashova, Natalia E. Grammatikova, Andrey E. Shchekotikhin, Pál Herczegh, Gyula Batta
Dátum:2021
ISSN:1424-8247
Megjegyzések:For some time, glycopeptide antibiotics have been considered the last line of defense against Methicillin-resistant Staphylococcus aureus (MRSA). However, vancomycin resistance of Gram-positive bacteria is an increasingly emerging worldwide health problem. The mode of action of glycopeptide antibiotics is essentially the binding of peptidoglycan cell-wall fragments terminating in the D-Ala-D-Ala sequence to the carboxylate anion binding pocket of the antibiotic. Dimerization of these antibiotics in aqueous solution was shown to persist and even to enhance the antibacterial effect in a co-operative manner. Some works based on solid state (ss) Nuclear Magnetic Resonance (NMR) studies questioned the presence of dimers under the conditions of ssNMR while in a few cases, higher-order oligomers associated with contiguous back-to-back and face-to-face dimers were observed in the crystal phase. However, it is not proved if such oligomers persist in aqueous solutions. With the aid of 15N-labelled eremomycin using 15N relaxation and diffusion NMR methods, we observed tetramers and octamers when the N-Ac-D-Ala-D-Ala dipeptide was added. To the contrary, the N-Ac-D-Ala or (N-Ac)2-L-Lys-D-Ala-D-Ala tripeptide did not induce higher-order oligomers. These observations are interesting examples of tailored supramolecular self-organization. New antimicrobial tests have also been carried out with these self-assemblies against MRSA and VRE (resistant) strains.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
glycopeptide
resistance
eremomycin
dimer
oligomer
N-Ac-D-Ala-D-Ala
ligand
15N relaxation
diffusion
NMR
Megjelenés:Pharmaceuticals. - 14 : 2 (2021), p. 1-14. -
További szerzők:Erdei Réka Tevyashova, Anna N. Grammatikova, Natalia E. Shchekotikhin, Andrey E. Herczegh Pál (1947-) (vegyész, antibiotikumkémikus) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:GINOP-2.3.2-15-2016-00008
GINOP
GINOP-2.3.3-15-2016-00004
GINOP
NKFIH K119509
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