Sulfated and non-sulfated glycopeptide recognition domains of P-selectin glycoprotein ligand 1 and their binding to P- and E-selectin.
Total synthesis through block glycosylation and selective chemical O-sulfation of tyrosine residues yielded the glycopeptide recognition domain A (X=SO(3) (-)) of the P-selectin glycoprotein ligand 1, in which the terminal sialic acid of the complex hexasaccharide side chain was replaced by (S)-cyclohexyl lactic acid. In binding assays the O-sulfated structure A showed high affinity towards P-selectin, the non-sulfated towards E-selectin.
Baumann
Katharina
K
Institut für Organische Chemie, Johannes Gutenberg-Universität Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
Kowalczyk
Danuta
D
Gutjahr
Tobias
T
Pieczyk
Markus
M
Jones
Claire
C
Wild
Martin K
MK
Vestweber
Dietmar
D
Kunz
Horst
H