化学
肽
二肽
表面等离子共振
肽序列
氨基酸
体外
生物化学
新生儿Fc受体
共识序列
肽库
寡肽
噬菌体展示
分子生物学
免疫球蛋白G
抗体
生物
基因
免疫学
材料科学
纳米颗粒
纳米技术
作者
Adam R. Mezo,Kevin McDonnell,Alfredo Castro,Cara Fraley
标识
DOI:10.1016/j.bmc.2008.05.004
摘要
A family of five peptides was previously discovered by phage display techniques that binds to the human neonatal Fc receptor (FcRn) and inhibits the human IgG:human FcRn protein-protein interaction [Proc. Nat. Acad. Sci. U.S.A.2008, 105, 2337-2342]. The consensus peptide motif consists of the sequence GHFGGXY where X is preferably a hydrophobic amino acid, and also includes a disulfide bridge enclosing 11-amino acids in varying positions about the consensus sequence. We describe herein the structure-activity relationships of one of the five peptides in binding to FcRn using surface plasmon resonance and IgG:FcRn competition ELISA assays. Modifications of the peptide length, cyclization, and the incorporation of amino acid substitutions and dipeptide mimetics were studied. The most potent analogs exhibited a 50- to 100-fold improvement of in vitro activity over that of the phage-identified peptide sequence.
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