Molecular Architecture with Functionalized β-Peptide Helices

摘要

Helical secondary structures are a fundamental part of protein architecture and are widely involved in recognition and binding processes between proteins or between proteins and nucleic acids. Furthermore, the organization of peptide helices in bundles is common for the membrane-spanning domains of transmembrane proteins and for many soluble proteins. Peptide helices can be used as templates for specific preorganization of peptides in ligation. The design of amphiphilic helices is important for model studies related to these complex biomolecular interactions. Among α-peptides usually about 15-20 amino acids are needed for significant degree of helical secondary structure in aqueous solution.