Specificity and affinity studies in lectin/ carbohydrate
interactions

C 2009

Specificity and affinity studies in lectin/ carbohydrate interactions

ŠULÁK, Ondřej, Emile LAMEIGNERE, Michaela WIMMEROVÁ and Anne IMBERTY

Basic information

Original name

Specificity and affinity studies in lectin/ carbohydrate interactions

Name in Czech

Studium specifity a afinity lektin/sacharidových interakcí

Authors

ŠULÁK, Ondřej (203 Czech Republic), Emile LAMEIGNERE (250 France), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution) and Anne IMBERTY (250 France)

Edition

35. vyd. UK, Carbohydrate Chemistry, p. 356-371, 16 pp. SPR Carbohydrate Chemistry, Vol. 35, 2009

Publisher

The Royal Society of Chemistry 2009

Other information

Language

English

Type of outcome

Kapitola resp. kapitoly v odborné knize

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Publication form

electronic version available online

RIV identification code

RIV/00216224:14310/09:00035557

Organization unit

Faculty of Science

ISBN

978-1-84755-880-0

DOI

http://dx.doi.org/10.1039/b901572h

UT WoS

000332290700014

Keywords (in Czech)

lektiny;ITC;SPR; fluorescence;NMR;interaction

Keywords in English

lectins; ITC; SPR; fluorescence; NMR; interaction

Abstract

ORIG CZ

V originále

Lectins are ubiquitous carbohydrate-binding proteins, characterized by their specificity recognition towards complex oligosaccharides and their non-immune origin.Their ability to distinguish oligosaccharides is central to many biological processes involving cell communication. They also play a role in many diseases being involved in cancer development and metastasis, inflammation and host-pathogen recognition. If recently characterized bacterial lectins display higher affinity for their target with Kd for monosaccharides in the micromolar range,3 lectin-carbohydrate interactions are more often characterized by rather low affinity, which is generally compensated by the presence of several binding sites, resulting in avidity or velcro effect. The development of fast and effective methods for determining lectin affinity and specificity has been hampered by the technical problem of obtaining sufficient amount of pure and well characterized oligosaccharides.

In Czech

Rewiew o současných možnostech studia lektin/sacharidových interakcí.

Links

LC06030, research and development project

Name: Biomolekulární centrum

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

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

ŠULÁK, Ondřej, Emile LAMEIGNERE, Michaela WIMMEROVÁ and Anne IMBERTY. Specificity and affinity studies in lectin/ carbohydrate interactions. Online. In Carbohydrate Chemistry. 35th ed. UK: The Royal Society of Chemistry 2009, 2009, p. 356-371. SPR Carbohydrate Chemistry, Vol. 35. ISBN 978-1-84755-880-0. Available from: https://dx.doi.org/10.1039/b901572h.

@inbook{832434,
   author = {Šulák, Ondřej and Lameignere, Emile and Wimmerová, Michaela and Imberty, Anne},
   address = {UK},
   booktitle = {Carbohydrate Chemistry},
   doi = {http://dx.doi.org/10.1039/b901572h},
   edition = {35},
   keywords = {lectins; ITC; SPR; fluorescence; NMR; interaction},
   howpublished = {elektronická verze "online"},
   language = {eng},
   location = {UK},
   isbn = {978-1-84755-880-0},
   pages = {356-371},
   publisher = {The Royal Society of Chemistry 2009},
   title = {Specificity and affinity studies in lectin/ carbohydrate interactions},
   year = {2009}
}

TY  - CHAP
ID  - 832434
AU  - Šulák, Ondřej - Lameignere, Emile - Wimmerová, Michaela - Imberty, Anne
PY  - 2009
TI  - Specificity and affinity studies in lectin/ carbohydrate interactions
VL  - SPR Carbohydrate Chemistry, Vol. 35
PB  - The Royal Society of Chemistry 2009
CY  - UK
SN  - 9781847558800
KW  - lectins
KW  - ITC
KW  - SPR
KW  - fluorescence
KW  - NMR
KW  - interaction
N2  - Lectins are ubiquitous carbohydrate-binding proteins, characterized by their specificity recognition towards complex oligosaccharides and their non-immune origin.Their ability to distinguish oligosaccharides is central to many biological processes involving cell communication. They also play a role in many diseases being involved in cancer development and metastasis, inflammation and host-pathogen recognition. If recently characterized bacterial lectins display higher affinity for their target with Kd for monosaccharides in the micromolar range,3 lectin-carbohydrate interactions are more often characterized by rather low affinity, which is generally compensated by the presence of several binding sites, resulting in avidity or velcro effect. The development of fast and effective methods for determining lectin affinity and specificity has been hampered by the technical problem of obtaining sufficient amount of pure and well characterized oligosaccharides.
ER  -

ŠULÁK, Ondřej, Emile LAMEIGNERE, Michaela WIMMEROVÁ and Anne IMBERTY. Specificity and affinity studies in lectin/ carbohydrate interactions. Online. In \textit{Carbohydrate Chemistry}. 35th ed. UK: The Royal Society of Chemistry 2009, 2009, p.~356-371. SPR Carbohydrate Chemistry, Vol. 35. ISBN~978-1-84755-880-0. Available from: https://dx.doi.org/10.1039/b901572h.

Detailed Information on Publication Record