MARROTE, Karine, Charles SABIN, Cathy PRÉVILLE, Myriam MOUMÉ-PYMBOCK, Michaela WIMMEROVÁ, Edward P. MITCHELL, Anne IMBERTY and René ROY. X-ray Structures and Thermodynamics of the Interaction of PA-IIL from Pseudomonas aeruginosa with Disaccharide Derivatives. ChemMedChem. Weinheim: WILEY-VCH Verlag GmbH & Co. KGaA, 2007, vol. 2, No 9, p. 1328-1338. ISSN 1860-7187.
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Basic information
Original name X-ray Structures and Thermodynamics of the Interaction of PA-IIL from Pseudomonas aeruginosa with Disaccharide Derivatives
Name in Czech X-ray struktury a termodynamika interakce lektinu PA-IIL z Pseudomonas aeruginosa s disacharidovými deriváty
Authors MARROTE, Karine (124 Canada), Charles SABIN (250 France), Cathy PRÉVILLE (124 Canada), Myriam MOUMÉ-PYMBOCK (124 Canada), Michaela WIMMEROVÁ (203 Czech Republic, guarantor), Edward P. MITCHELL (826 United Kingdom of Great Britain and Northern Ireland), Anne IMBERTY (250 France) and René ROY (124 Canada).
Edition ChemMedChem, Weinheim, WILEY-VCH Verlag GmbH & Co. KGaA, 2007, 1860-7187.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 2.825
RIV identification code RIV/00216224:14310/07:00022341
Organization unit Faculty of Science
UT WoS 000249500800011
Keywords in English Pseudomonas aeruginosa; lectin; inhibitors; structure; thermodynamics
Tags inhibitors, lectin, Pseudomonas aeruginosa, structure, Thermodynamics
Tags International impact, Reviewed
Changed by Changed by: prof. RNDr. Michaela Wimmerová, Ph.D., učo 854. Changed: 1/9/2007 08:33.
Abstract
Pseudomonas aeruginosa is an opportunistic bacterium showing increasing resistance to antibiotics and consequently represents elevated threatening problems in hospital environments, particularly for cystic fibrosis patients. The use of glycomimetics as an anti-adhesive strategy against microorganisms may complement the use of antibiotherapies. PA-IIL lectin (LecB) from P.aeruginosa constitutes an appealing target for antibacterial agents, as it has been proposed to play a key role in binding to airway epithelia and/or to be involved in biofilm formation. The lectin has an unusually high affinity for l-fucose and related oligosaccharides. In the work presented herein, the disaccharide aFuc1-4GlcNAc is used as a scaffold toward the synthesis of a series of glycomimetic derivatives. Microcalorimetry and structural studies indicate that several of the derivatives are potent inhibitors of the lectin, with affinity in the same range as the best known natural ligand, Lewis a, and could represent interesting leads for the development of future antibacterial compounds.
Abstract (in Czech)
X-ray struktury a termodynamika interakce lektinu PA-IIL z Pseudomonas aeruginosa s disacharidovými deriváty
Links
LC06030, research and development projectName: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
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