四斯潘宁
CD81号
转移
癌症转移
癌细胞
癌症
癌症研究
化学
细胞
纳米技术
计算生物学
生物
生物化学
材料科学
遗传学
丙型肝炎病毒
病毒
作者
Kun Xu,Han Gao,Yongming Li,Yulong Jin,Rui Zhao,Yanyan Huang
标识
DOI:10.1002/anie.202400129
摘要
Probing biomolecular interactions at cellular interfaces is crucial for understanding and interfering with life processes. Although affinity binders with site specificity for membrane proteins are unparalleled molecular tools, a high demand remains for novel multi-functional ligands. In this study, a synthetic peptide (APQQ) with tight and specific binding to the untargeted extracellular loop of CD81 evolved from a genetically encoded peptide pool. With tailored affinity, APQQ flexibly accesses, site-specifically binds, and forms a complex with CD81, enabling in-situ tracking of the dynamics and activity of this protein in living cells, which has rarely been explored because of the lack of ligands. Furthermore, APQQ triggers the relocalization of CD81 from diffuse to densely clustered at cell junctions and modulates the interplay of membrane proteins at cellular interfaces. Motivated by these, efficient suppression of cancer cell migration, and inhibition of breast cancer metastasis were achieved in vivo.
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