β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers

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42

摘要:

Chemists have long sought to extrapolate the power of biological catalysis and recognition to synthetic systems. These efforts have focused largely on low molecular weight catalysts and receptors; however, biological systems themselves rely almost exclusively on polymers, proteins and RNA, to perform complex chemical functions. Proteins and RNA are unique in their ability to adopt compact, well-ordered conformations, and specific folding provides precise spatial orientation of the functional groups that comprise the "active site". These features suggest that identification of new polymer backbones with discrete and predictable folding propensities ("foldamers") will provide a basis for design of molecular machines with unique capabilities. The foldamer approach complements current efforts to design unnatural properties into polypeptides and polynucleotides. The first step in creating a foldamer is to identify polymeric backbones with well-defined secondary structural preferences. Here we describe a new polyamide family (1—5) that strongly favors a specific helical secondary structure, which should ultimately serve as a building block for stable tertiary structures.

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DOI:

10.2337/db05-1230

年份:

1996

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