期刊
CHEMBIOCHEM
卷 12, 期 7, 页码 1035-1038出版社
WILEY-BLACKWELL
DOI: 10.1002/cbic.201000753
关键词
beta-amino acid; foldamers; helical bundles; peptides; protein engineering
资金
- NSF
- Yale Center
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0848098] Funding Source: National Science Foundation
We reported recently that certain beta(3)-peptides self-assemble in aqueous solution into discrete bundles of unique structure and defined stoichiometry. The first beta-peptide bundle reported was the octameric Zwit-1F, whose fold is characterized by a well-packed, leucine-rich core and a salt-bridge-rich surface. Close inspection of the Zwit-1F structure revealed four nonideal interhelical salt-bridge interactions whose heavy atom-heavy atom distances were longer than found in natural proteins of known structure. Here we demonstrate that the thermodynamic stability of a beta-peptide bundle can be enhanced by optimizing the length of these four interhelical salt bridges. Combined with previous work on the role of internal packing residues, these results provide another critical step in the bottom-up formation of beta-peptide assemblies with defined sizes, reproducible structures, and sophisticated function.
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