A family of concanavalin A-binding peptides from a hexapeptide epitope library.
| dc.creator | Scott, J K | |
| dc.creator | Loganathan, D | |
| dc.creator | Easley, R B | |
| dc.creator | Gong, X | |
| dc.creator | Goldstein, I J | |
| dc.date | 1992-06-15 | |
| dc.date.accessioned | 2026-08-03T01:35:59Z | |
| dc.description | The lectin concanavalin A (Con A) binds methyl alpha-D-mannopyranoside (Me alpha Man) as well as alpha-D-mannosyl groups at the nonreducing terminus of oligosaccharides. Ligand peptides that mimic the binding of Me alpha Man to Con A were identified from screening an epitope library composed of filamentous phage displaying random hexapeptides. A consensus sequence was identified among affinity-purified phage; Con A binds phage bearing this sequence and is inhibited from doing so by Me alpha Man. When tested for binding against a panel of lectins, phage bearing this sequence bind only weakly to a closely related D-mannose-binding lectin, indicating that binding to Con A is highly selective. A synthetic peptide bearing the consensus sequence blocks the precipitation of Con A by dextran with an inhibition strength equivalent to that of methyl alpha-D-glucopyranoside. These results demonstrate that the specificity of Con A is not limited to carbohydrates and that highly selective sugar-mimics for lectins of plant, animal, or bacterial origin may be identified from epitope libraries. | |
| dc.identifier | https://pmc.ncbi.nlm.nih.gov/articles/PMC49299/ | |
| dc.identifier | https://pubmed.ncbi.nlm.nih.gov/1376919/ | |
| dc.identifier | https://doi.org/10.1073/pnas.89.12.5398 | |
| dc.identifier.uri | https://repo.dare.co.zw/handle/123456789/156448 | |
| dc.language | en | |
| dc.publisher | National Academy of Sciences | |
| dc.source | Proc Natl Acad Sci U S A | |
| dc.subject | Research Article | |
| dc.title | A family of concanavalin A-binding peptides from a hexapeptide epitope library. | |
| dc.type | Text |