PEPTIDE LIGANDS FOR A SUGAR-BINDING PROTEIN ISOLATED FROM A RANDOM PEPTIDE LIBRARY
PEPTIDE LIGANDS FOR A SUGAR-BINDING PROTEIN ISOLATED FROM A RANDOM PEPTIDE LIBRARY
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DOI：
10.1073/pnas.89.12.5393
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发表时间：
1992-06-15
影响因子：
11.1
通讯作者：
GALLOP, MA
中科院分区：
文献类型：
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作者：
OLDENBURG, KR;LOGANATHAN, D;GALLOP, MA
糖结合蛋白伴刀豆球蛋白A（Con A）的肽配体已通过筛选在丝状噬菌体表面表达的大的、多样的肽库来鉴定。发现含有共有序列Tyr-Pro-Tyr的十二肽以46 μ M的亲和力（解离常数，K（d））结合Con A，与已知的碳水化合物配体甲基α-D-吡喃甘露糖苷（K（d）为89 μ M）的亲和力相当。此外，该肽抑制Con A对α-葡聚糖葡聚糖1355的沉淀。鉴于寡糖合成的复杂性，发现竞争性抑制碳水化合物特异性受体的肽的前景可能简化新治疗剂的开发。
Peptide ligands for the carbohydrate-binding protein concanavalin A (Con A) have been identified by screening a large, diverse peptide library expressed on the surface of filamentous phage. A dodecapeptide containing the consensus sequence Tyr-Pro-Tyr was found to bind Con A with an affinity (dissociation constant, K(d)) of 46-mu-M, comparable to that of a known carbohydrate ligand, methyl alpha-D-mannopyranoside (K(d) of 89-mu-M). In addition the peptide inhibited precipitation of the alpha-glucan dextran 1355 by Con A. Given the complexity of oligosaccharide synthesis, the prospect of finding peptides that competitively inhibit carbohydrate-specific receptors may simplify the development of new therapeutic agents.