6436-90-4Relevant articles and documents
EIF4E INHIBITORS AND USES THEREOF
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Paragraph 00337; 00363; 00373, (2021/09/11)
The present invention provides compounds inhibiting elF4E activity and compositions and methods of using thereof.
Structure-property relationship study of n-(hydroxy)peptides for the design of self-assembled parallel β-sheets
Roche, Stéphane P.,Richaud, Alexis D.
, p. 12329 - 12342 (2020/11/10)
The design of novel and functional biomimetic foldamers remains a major challenge in creating mimics of native protein structures. Herein, we report the stabilization of a remarkably short β-sheet by incorporating N-(hydroxy)glycine (Hyg) residues into the backbone of peptides. These peptide- peptoid hybrids form unique parallel β-sheet structures by selfassembly upon hydrogenation. Our spectroscopic and crystallographic data suggest that the local conformational perturbations induced by N-(hydroxy)amides are outweighed by a network of strong interstrand hydrogen bonds.
Selective Functionalization of Aliphatic Amines via Myoglobin-Catalyzed Carbene N-H Insertion
Fasan, Rudi,Sreenilayam, Gopeekrishnan,Steck, Viktoria
, p. 224 - 229 (2020/02/15)
Engineered myoglobins have recently gained attention for their ability to catalyze a variety of abiological carbene transfer reactions including the functionalization of amines via carbene insertion into N-H bonds. However, the scope of myoglobin and other hemoprotein-based biocatalysts in the context of this transformation has been largely limited to aniline derivatives as the amine substrates and ethyl diazoacetate as the carbene donor reagent. In this report, we describe the development of an engineered myoglobin-based catalyst that is useful for promoting carbene N-H insertion reactions across a broad range of substituted benzylamines and α-diazo acetates with high efficiency (82-99percent conversion), elevated catalytic turnovers (up to 7,000), and excellent chemoselectivity for the desired single insertion product (up to 99percent). The scope of this transformation could be extended to cyclic aliphatic amines. These studies expand the biocatalytic toolbox available for the selective formation of C-N bonds, which are ubiquitous in many natural and synthetic bioactive compounds.