Selection and syntheses of tentacle type peptides as 'artificial' lectins against various cell-surface carbohydrates.
Sialyl Lewis X and its derivatives are cell-surface carbohydrates that are involved in cell-cell recognition by carbohydrate-mediated interactions. Unfortunately, owing to the similarities between carbohydrates only a limited number of tools are available for their differentiation. In this study, we prepared a selected phage-displayed peptide library against LeX (2), SLN (3), or LN (4), which compared to sLeX (1) lack sialic acid, fucose, and both sialic acid and fucose from constituents, respectively. Sequences of the selected peptides, prepared as tentacle type dimeric peptides, were prepared and shown to have micromolar affinities for the cognate carbohydrates. The specificities displayed by these 'artificial' lectins overwhelm those of natural lectins. These results suggest that they can serve as useful tools to detect changes in the terminal monosaccharide of cell-surface carbohydrates.
Hyun
Soonsil
S
Department of Chemistry and Education, Seoul National University, Seoul 151-742, Republic of Korea.
Kim
Jiyoung
J
Kwon
Miyun
M
Yu
Jaehoon
J
D001665:Binding Sites; D001667:Binding, Competitive; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002462:Cell Membrane / Q000737:chemistry; D037102:Lectins / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000037:antagonists & inhibitors*; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D037102:Lectins; D009844:Oligosaccharides; D019151:Peptide Library; D010455:Peptides