Studies on the interaction of the antibiotic moenomycin A with the enzyme penicillin-binding protein 1b

Autor:	Juan A. Ayala, Lothar Hennig, Thomas Rühl, Andrij Buchynskyy, Peter Welzel, Ramona Oehme, Dietmar Knoll, Matthias Findeisen, Sabine Giesa, Daniela Volke, Karen Barche, Uwe Kempin, Mohammed Daghish, Katherina Stembera
Rok vydání:	2003
Předmět:	Peptidyl transferase Penicillin binding proteins Octoxynol Stereochemistry Clinical Biochemistry Pharmaceutical Science Microbial Sensitivity Tests Plasma protein binding Muramoylpentapeptide Carboxypeptidase Biochemistry Diffusion Muramoylpentapeptide carboxypeptidase Bacterial Proteins Drug Discovery polycyclic compounds Penicillin-Binding Proteins Binding site Nuclear Magnetic Resonance Biomolecular Molecular Biology Antibacterial agent chemistry.chemical_classification biology Chemistry Organic Chemistry biochemical phenomena metabolism and nutrition Anti-Bacterial Agents Bambermycins Spectrometry Fluorescence Enzyme Hexosyltransferases Peptidyl Transferases biology.protein Molecular Medicine Carrier Proteins Protein Binding Conjugate
Zdroj:	Bioorganic & Medicinal Chemistry. 11:2965-2981
ISSN:	0968-0896
DOI:	10.1016/s0968-0896(03)00187-1
Popis:	The interaction of a moenomycin derivative with the enzyme penicillin binding protein 1b (PBP 1b) has been studied by means of STD NMR. The results obtained initiated the synthesis of a number of moenomycin derivatives modified in unit A including a moenomycin-ampicillin conjugate and determination of their antibiotic activities. A protocol is described that allows studying the interaction of moenomycin analogues with PBP 1b by fluorescence correlation spectroscopy.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::512e7c25dc840d2abd5d4b892bebecc5 https://doi.org/10.1016/s0968-0896(03)00187-1 Zobrazit plný text záznamu Full Text from ScienceDirect