Exploration of beta-turn scaffolding motifs as components of sialyl Le(X) mimetics and their relevance to P-selectin.
Monocyclic and bicyclic lactam units representing beta-turn surrogates were incorporated into a sialyl Le(X) structure by replacement of the natural sugar components. Low micromolar activity was found in a new P-selectin binding assay.
Hanessian
S
S
Department of Chemistry, Université de Montréal, Centre-ville, Montréal, Québec, Canada.
Huynh
H K
HK
Reddy
G V
GV
McNaughton-Smith
G
G
Ernst
B
B
Kolb
H C
HC
Magnani
J
J
Sweeley
C
C
D001667:Binding, Competitive; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D019040:E-Selectin / Q000378:metabolism; D007212:Indolizines / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D019007:P-Selectin / Q000378:metabolism*; D000080506:Sialyl Lewis X Antigen; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D047090:beta-Lactams / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*
D019040:E-Selectin; D007212:Indolizines; D009844:Oligosaccharides; D019007:P-Selectin; D000080506:Sialyl Lewis X Antigen; D047090:beta-Lactams