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Identification of a novel N-cadherin antagonist.

机译:新型N-钙粘蛋白拮抗剂的鉴定。

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The cell adhesion molecule, N-cadherin plays a pivotal role in many biological and disease processes. Drugs that modulate N-cadherin function should therefore be useful therapeutic agents. We have used phage display technology to identify amino acid sequences capable of binding to N-cadherin. All of these sequences harbor a Trp residue in the second position from the N-terminus. A synthetic linear peptide containing one of these sequences, H-SWTLYTPSGQSK-NH(2) was found to bind a chimeric protein composed of the N-cadherin ectodomain fused to the immunoglobulin G1 Fc fragment with an affinity (K(D)) of 10.7muM, as determined by surface plasmon resonance. It also blocked the aggregation of beads coated with this chimeric protein. Furthermore, this peptide disrupted adhesion and tube formation by N-cadherin-expressing human umbilical vein endothelial cells in vitro. These observations suggest that N-cadherin antagonists have the potential of serving as anti-angiogenic agents. The peptide, H-SWTLYTPSGQSK-NH(2) should prove useful for studies designed to evaluate N-cadherin function in various biological processes.
机译:细胞粘附分子N-钙粘着蛋白在许多生物学和疾病过程中起着关键作用。因此,调节N-钙粘蛋白功能的药物应该是有用的治疗剂。我们已经使用噬菌体展示技术来鉴定能够结合N-钙粘蛋白的氨基酸序列。所有这些序列都在N末端的第二个位置带有一个Trp残基。发现包含这些序列之一的合成线性肽H-SWTLYTPSGQSK-NH(2)以10.7的亲和力(K(D))结合由与免疫球蛋白G1 Fc片段融合的N-钙粘蛋白胞外域组成的嵌合蛋白。 μM,由表面等离振子共振确定。它也阻止了包被这种嵌合蛋白的珠的聚集。此外,该肽在体外破坏了表达N-钙粘蛋白的人脐静脉内皮细胞的粘附和管形成。这些观察结果表明,N-钙粘蛋白拮抗剂具有用作抗血管生成剂的潜力。 H-SWTLYTPSGQSK-NH(2)肽应被证明对评估各种生物过程中N-钙粘蛋白功能的研究有用。

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