Synthesis and biological evaluation of sperm CD52 GPI anchor and related derivatives as binding receptors of pore-forming CAMP factor.
Sperm CD52 GPI anchor and its derivatives containing different carbohydrate chains were prepared in a highly convergent fashion starting from the same properly protected phospholipidated pseudodisaccharide. Coupling this common key intermediate to various oligosaccharyl donors quickly afforded the framework of the synthetic targets, which was followed by global deprotection to furnish the desired structures. Preliminary studies on the biological properties of the synthetic GPI derivatives indicated that both the intact GPI anchor and the free phospholipidated pseudodisaccharide interacted strongly with CAMP factor, a pore-forming bacterial toxin.
Wu
Xiaoming
X
Department of Chemistry, Wayne State University, Detroit, MI 48202, USA.
Shen
Zhihong
Z
Zeng
Xiangqun
X
Lang
Shenhui
S
Palmer
Michael
M
Guo
Zhongwu
Z
D015703:Antigens, CD / Q000378:metabolism*; D000951:Antigens, Neoplasm / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D000074301:CD52 Antigen; D006023:Glycoproteins / Q000138:chemical synthesis* / Q000378:metabolism*; D017261:Glycosylphosphatidylinositols / Q000138:chemical synthesis* / Q000378:metabolism*; D006460:Hemolysin Proteins / Q000378:metabolism*; D006801:Humans; D008297:Male; D013094:Spermatozoa / Q000737:chemistry
D015703:Antigens, CD; D000951:Antigens, Neoplasm; D001426:Bacterial Proteins; C039092:CAMP protein, Streptococcus; D000074301:CD52 Antigen; C000613862:CD52 protein, human; D006023:Glycoproteins; D017261:Glycosylphosphatidylinositols; D006460:Hemolysin Proteins