Abstract
The syntheses of five natural and N-terminal acetylated peptides and glycopeptides of the CD52 antigen are described. Solid phase peptide synthesis was employed in the construction of the target compounds from Fmoc-protected commercial amino acids and synthetic glycan-asparagine conjugates. Circular dichroism studies of the synthetic targets showed that they exist as random coils in solution, and no significant change in secondary structure was observed when the CD52 peptide was either acetylated at the N-terminus or glycosylated at the Asn(3) residue with a disaccharide or a fucose-containing branched trisaccharide.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Antigens, CD / chemistry*
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Antigens, Neoplasm / chemistry*
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CD52 Antigen
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Carbohydrate Conformation
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Circular Dichroism / methods
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Disaccharides / chemistry
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Fucose / analysis
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Fucose / chemistry
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Glycopeptides / chemical synthesis
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Glycopeptides / chemistry*
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Glycoproteins / chemical synthesis
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Glycoproteins / chemistry*
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Models, Molecular
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Molecular Conformation
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry*
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Oligosaccharides / chemistry
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Trisaccharides / chemistry
Substances
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Antigens, CD
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Antigens, Neoplasm
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CD52 Antigen
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Disaccharides
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Glycopeptides
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Glycoproteins
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Oligopeptides
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Oligosaccharides
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Trisaccharides
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Fucose