Specificity and affinity studies in lectin/ carbohydrate
interactions

C 2009

Specificity and affinity studies in lectin/ carbohydrate interactions

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

Základní údaje

Originální název

Specificity and affinity studies in lectin/ carbohydrate interactions

Název česky

Studium specifity a afinity lektin/sacharidových interakcí

Autoři

ŠULÁK, Ondřej (203 Česká republika), Emile LAMEIGNERE (250 Francie), Michaela WIMMEROVÁ (203 Česká republika, garant, domácí) a Anne IMBERTY (250 Francie)

Vydání

35. vyd. UK, Carbohydrate Chemistry, od s. 356-371, 16 s. SPR Carbohydrate Chemistry, Vol. 35, 2009

Nakladatel

The Royal Society of Chemistry 2009

Další údaje

Jazyk

angličtina

Typ výsledku

Kapitola resp. kapitoly v odborné knize

Obor

10600 1.6 Biological sciences

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Forma vydání

elektronická verze "online"

Kód RIV

RIV/00216224:14310/09:00035557

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-1-84755-880-0

DOI

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

UT WoS

000332290700014

Klíčová slova česky

lektiny;ITC;SPR; fluorescence;NMR;interaction

Klíčová slova anglicky

lectins; ITC; SPR; fluorescence; NMR; interaction

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 24. 6. 2020 09:53, Mgr. Marie Šípková, DiS.

Anotace

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.

Česky

Rewiew o současných možnostech studia lektin/sacharidových interakcí.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

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

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