Powell Wyatt C, Evenson Garrett E, Walczak Maciej A
Department of Chemistry, University of Colorado, Boulder, Colorado 80309, United States.
ACS Catal. 2022 Jul 1;12(13):7789-7797. doi: 10.1021/acscatal.2c01938. Epub 2022 Jun 16.
Direct peptide and protein activation is a challenging transformation because of the stabilizing effect of the amide group. While enzymes can be considered as prototypical systems that have evolved to achieve high selectivity and specificity, small-molecule catalysts that functionalize the amide group may accommodate a much larger selection of substrates but currently remain scarce. Here, by combining the desired features from both catalytic regimes we designed an artificial cyclodehydratase, a catalytic system for the site-selective modification of peptides and natural products by engrafting heterocycles into their scaffolds. The catalytic system features a molybdenum(VI) center that was decorated with a sterically congested tripod ligand. The optimized catalyst can introduce azolines into small molecules, natural products, and oligopeptides with high efficiency and minimal waste. We further demonstrate the utility of the new protocol in the direct functionalization of a single amide group in the presence of up to seven other chemically similar positions and in the direct conversion of these groups into amines and thioamides. This new mechanistic paradigm may address an unmet need for a general method for the selective and sustainable functionalization of peptides and natural products.
由于酰胺基团的稳定作用,直接进行肽和蛋白质的活化是一项具有挑战性的转化过程。虽然酶可被视为已进化以实现高选择性和特异性的典型体系,但能使酰胺基团功能化的小分子催化剂可适用的底物选择范围要大得多,然而目前这类催化剂仍然稀少。在此,通过结合两种催化机制的所需特性,我们设计了一种人工环化脱水酶,这是一种通过将杂环嫁接到肽和天然产物的支架上,对其进行位点选择性修饰的催化体系。该催化体系的特征是一个钼(VI)中心,其带有一个空间位阻较大的三脚架配体。优化后的催化剂能够高效且低浪费地将唑啉引入小分子、天然产物和寡肽中。我们进一步证明了该新方法在多达七个其他化学性质相似的位置存在时对单个酰胺基团进行直接功能化,以及将这些基团直接转化为胺和硫代酰胺方面的实用性。这种新的机制范式可能满足了对肽和天然产物进行选择性和可持续功能化的通用方法这一未满足的需求。