X-ray Structures and Thermodynamics of the Interaction of
PA-IIL from Pseudomonas aeruginosa with Disaccharide
Derivatives

J 2007

X-ray Structures and Thermodynamics of the Interaction of PA-IIL from Pseudomonas aeruginosa with Disaccharide Derivatives

MARROTE, Karine, Charles SABIN, Cathy PRÉVILLE, Myriam MOUMÉ-PYMBOCK, Michaela WIMMEROVÁ et. al.

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

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

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

Abstract

ORIG CZ

V originále

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.

In Czech

X-ray struktury a termodynamika interakce lektinu PA-IIL z Pseudomonas aeruginosa s disacharidovými deriváty

Links

LC06030, research and development project

Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

Citovat

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.

@article{720870,
   author = {Marrote, Karine and Sabin, Charles and Préville, Cathy and MouméandPymbock, Myriam and Wimmerová, Michaela and Mitchell, Edward P. and Imberty, Anne and Roy, René},
   article_location = {Weinheim},
   article_number = {9},
   keywords = {Pseudomonas aeruginosa; lectin; inhibitors; structure; thermodynamics},
   language = {eng},
   issn = {1860-7187},
   journal = {ChemMedChem},
   title = {X-ray Structures and Thermodynamics of the Interaction of PA-IIL from Pseudomonas aeruginosa with Disaccharide Derivatives},
   volume = {2},
   year = {2007}
}

TY  - JOUR
ID  - 720870
AU  - Marrote, Karine - Sabin, Charles - Préville, Cathy - Moumé-Pymbock, Myriam - Wimmerová, Michaela - Mitchell, Edward P. - Imberty, Anne - Roy, René
PY  - 2007
TI  - X-ray Structures and Thermodynamics of the Interaction of PA-IIL from Pseudomonas aeruginosa with Disaccharide Derivatives
JF  - ChemMedChem
VL  - 2
IS  - 9
SP  - 1328-1338
EP  - 1328-1338
PB  - WILEY-VCH Verlag GmbH & Co. KGaA
SN  - 18607187
KW  - Pseudomonas aeruginosa
KW  - lectin
KW  - inhibitors
KW  - structure
KW  - thermodynamics
N2  - 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.
ER  -

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. \textit{ChemMedChem}. Weinheim: WILEY-VCH Verlag GmbH \&{} Co. KGaA, 2007, vol.~2, No~9, p.~1328-1338. ISSN~1860-7187.

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