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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F09%3A00327089%21RIV10-MSM-61388971
rdf:type
skos:Concept n13:Vysledek
dcterms:description
Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectinmediated cell adhesion to extra-cellular matrix (ECM) proteins. We here present the biofunctionalization of surfaces with poly-LacNAc structures and subsequent binding of ECM glycoproteins. First, we synthesized β-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human β1,4-galactosyl-transferase-1 and β1,3-N-acetylglucosaminyltransferase from Helicobacter pylori. These compounds were also used for kinetic characterization of glycosyltransferases and lectin binding assays. A mixture of poly-LacNAc-structures covalently coupled to functionalized microtiter plates were identified for best binding to our model galectin His6CGL2 Poly-N-acetyllactosamine (poly-LacNAc) structures have been identified as important ligands for galectinmediated cell adhesion to extra-cellular matrix (ECM) proteins. We here present the biofunctionalization of surfaces with poly-LacNAc structures and subsequent binding of ECM glycoproteins. First, we synthesized β-GlcNAc glycosides carrying a linker for controlled coupling onto chemically functionalized surfaces. Then we produced poly-LacNAc structures with defined lengths using human β1,4-galactosyl-transferase-1 and β1,3-N-acetylglucosaminyltransferase from Helicobacter pylori. These compounds were also used for kinetic characterization of glycosyltransferases and lectin binding assays. A mixture of poly-LacNAc-structures covalently coupled to functionalized microtiter plates were identified for best binding to our model galectin His6CGL2
dcterms:title
Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces
skos:prefLabel
Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces Chemo-enzymatic synthesis of poly-N-acetyllactosamine (poly-LacNAc) structures and their characterization for CGL2-galectin-mediated binding of ECM glycoproteins to biomaterial surfaces
skos:notation
RIV/61388971:_____/09:00327089!RIV10-MSM-61388971
n3:aktivita
n9:Z n9:P
n3:aktivity
P(IAA400200503), P(LC06010), Z(AV0Z50200510)
n3:cisloPeriodika
2
n3:dodaniDat
n15:2010
n3:domaciTvurceVysledku
n8:5894190 n8:7346689 n8:7203993
n3:druhVysledku
n18:J
n3:duvernostUdaju
n11:S
n3:entitaPredkladatele
n5:predkladatel
n3:idSjednocenehoVysledku
306923
n3:idVysledku
RIV/61388971:_____/09:00327089
n3:jazykVysledku
n17:eng
n3:klicovaSlova
chemo-enzymatic sysnthesis; galectin binding; biomaterials
n3:klicoveSlovo
n6:galectin%20binding n6:biomaterials n6:chemo-enzymatic%20sysnthesis
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[6C3837874424]
n3:nazevZdroje
Glycoconjugate Journal
n3:obor
n4:EE
n3:pocetDomacichTvurcuVysledku
3
n3:pocetTvurcuVysledku
7
n3:projekt
n14:LC06010 n14:IAA400200503
n3:rokUplatneniVysledku
n15:2009
n3:svazekPeriodika
26
n3:tvurceVysledku
Sauerzapfe, B. Pelantová, Helena Křenek, Karel Elling, L. Wakarchuk, W. W. Křen, Vladimír Schmiedel, J.
n3:wos
000263417500003
n3:zamer
n10:AV0Z50200510
s:issn
0282-0080
s:numberOfPages
18