Residue selective crosslinking of proteins through photoactivatable or proximity-enabled reactivity.
Residue selective crosslinking of proteins through photoactivatable or proximity-enabled reactivity.
复制标题
DOI：
10.1016/j.cbpa.2023.102285
复制
发表时间：
2023-03
影响因子：
7.8
通讯作者：
Jun Liu;Bin Yang;Lei Wang
中科院分区：
文献类型：
--
作者：
Jun Liu;Bin Yang;Lei Wang
蛋白质的光交联和化学交联为研究蛋白质结构和蛋白质与生物分子的相互作用提供了多种途径。传统的光活化基团通常对氨基酸残基缺乏反应选择性。最近出现了新的光活化基团与选定的残基反应，提高了交联效率并促进了交联鉴定。传统的化学交联通常采用高活性官能团，而最近的研究进展则开发了具有接近性的潜在活性基团，减少了虚假交联，提高了生物相容性。综述了这些由光或邻近激活的残基选择性化学官能团在小分子交联剂和遗传编码的非天然氨基酸中的应用。随着鉴定蛋白质交联的新软件开发，残基选择性交联增强了在体外、细胞裂解液和活细胞中难以捉摸的蛋白质-蛋白质相互作用的研究。残基选择性交联有望扩展到研究各种蛋白质-生物分子相互作用的其他方法。
Photo- and chemical crosslinking of proteins have offered various avenues for studying protein structure and protein interactions with biomolecules. Conventional photoactivatable groups generally lack reaction selectivity toward amino acid residues. New photoactivatable groups reacting with selected residues have emerged recently, increasing crosslinking efficiency and facilitating crosslink identification. Traditional chemical crosslinking usually employs highly reactive functional groups, while recent advance has developed latent reactive groups with reactivity triggered by proximity, which reduce spurious crosslinks and improve biocompatibility. The employment of these residue selective chemical functional groups, activated by light or proximity, in small molecule crosslinkers and in genetically encoded unnatural amino acids is summarized. Together with new software development in identifying protein crosslinks, residue selective crosslinking has enhanced the research of elusive protein-protein interactions in vitro, in cell lysate, and in live cells. Residue selective crosslinking is expected to expand to other methods for the investigation of various protein–biomolecule interactions.