ABSTRACT
Molecules that fold to mimic protein secondary structures have emerged as important targets of bioorganic chemistry. Recently, a variety of compounds that mimic helices, turns, and sheets have been developed, with notable advances in the design of beta-peptides that mimic each of these structures. These compounds hold promise as a step toward synthetic molecules with protein-like properties and as drugs that block protein-protein interactions.
Subject(s)
Drug Design , Protein Structure, Secondary , Proteins/chemical synthesis , Carbohydrate Sequence , Molecular Mimicry , Molecular Sequence Data , Peptides/chemistry , Proteins/chemistryABSTRACT
Within the past few years, a variety of compounds that mimic biopolymers have been developed. All of these unnatural oligomers are prepared by iterative syntheses, which are amenable to combinatorial strategies. Peptides continue to be popular targets for mimicry, and there is growing interest in targeting oligosaccharides. The incorporation of unnatural oligomers into compounds that adopt defined structures, such as helices or sheets, has emerged as an exciting new area of unnatural oligomer research.