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Peptide Folding and Binding Probed by Systematic Non-canonical Mutagenesis.
Frontiers in Molecular Biosciences ( IF 5 ) Pub Date : 2020-05-04 , DOI: 10.3389/fmolb.2020.00100
Joseph M Rogers 1
Affiliation  

Many proteins and peptides fold upon binding another protein. Mutagenesis has proved an essential tool in the study of these multi-step molecular recognition processes. By comparing the biophysical behavior of carefully selected mutants, the concert of interactions and conformational changes that occur during folding and binding can be separated and assessed. Recently, this mutagenesis approach has been radically expanded by deep mutational scanning methods, which allow for many thousands of mutations to be examined in parallel. Furthermore, these high-throughput mutagenesis methods have been expanded to include mutations to non-canonical amino acids, returning peptide structure-activity relationships with unprecedented depth and detail. These developments are timely, as the insights they provide can guide the optimization of de novo cyclic peptides, a promising new modality for chemical probes and therapeutic agents.



中文翻译:

通过系统性非规范诱变探测肽折叠和结合。

许多蛋白质和肽在结合另一种蛋白质时会折叠。诱变已被证明是研究这些多步分子识别过程的重要工具。通过比较精心挑选的突变体的生物物理行为,可以分离和评估折叠和结合过程中发生的相互作用和构象变化。最近,这种诱变方法已经通过深度突变扫描方法得到了根本性的扩展,该方法允许并行检查数千个突变。此外,这些高通量诱变方法已经扩展到包括非规范氨基酸的突变,以前所未有的深度和细节返回肽的结构-活性关系。这些发展是及时的,因为它们提供的见解可以指导优化从头 环肽,化学探针和治疗剂的一种有前途的新形式。

更新日期:2020-06-24
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