188540-42-3Relevant articles and documents
Multicomponent Peptide Stapling as a Diversity-Driven Tool for the Development of Inhibitors of Protein–Protein Interactions
Ali, Ameena M.,Atmaj, Jack,D?mling, Alexander,Groves, Matthew,Holak, Tad A.,Labuzek, Beata,Neochoritis, Constantinos G.,Plewka, Jacek,Ricardo, Manuel G.,Rivera, Daniel G.,Skalniak, Lukasz,Surmiak, Ewa,Zhang, Ran
supporting information, p. 5235 - 5241 (2020/02/15)
Stapled peptides are chemical entities in-between biologics and small molecules, which have proven to be the solution to high affinity protein–protein interaction antagonism, while keeping control over pharmacological performance such as stability and mem
Rapid generation of macrocycles with natural-product-like side chains by multiple multicomponent macrocyclizations (MiBs)
Rivera, Daniel G.,Vercillo, Otilie E.,Wessjohann, Ludger A.
experimental part, p. 1787 - 1795 (2008/10/09)
A small parallel library of peptoid macrocycles with natural-product- derived side chains of biological importance was produced by Ugi-type multiple multicomponent macrocyclizations including bifunctional building blocks (Ugi-MiBs). Diverse exocyclic elements of high relevance in natural recognition processes, i.e., all functional amino acid residues (e.g., Cys, Arg, His, Trp) and even sugar moieties, can be introduced in a one-pot process into different types of peptoid-containing macrocyclic skeletons. This is exemplified by the use of a diamine/diisocyanide combination of Ugi-MiBs and N-protected α-amino acids or carboxy-functionalized carbohydrates as source for the natural-product-like exocyclic elements. Employed as the acid components of the multiple Ugi reactions, they appear as N-amide substituents on the macrocyclic cores. The use of different diamines and diisocyanides allows an easy variation of the N- to C-directionality and therefore of the position of the exocyclic elements. The Royal Society of Chemistry.
