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Enhancing β 3 ‐Peptide Bundle Stability by Design
Author(s) -
Craig Cody J.,
Goodman Jessica L.,
Schepartz Alanna
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000753
Subject(s) - peptide , bundle , chemistry , aqueous solution , crystallography , salt bridge , helix bundle , salt (chemistry) , stoichiometry , protein structure , materials science , mutant , biochemistry , composite material , gene
We reported recently that certain β 3 ‐peptides self‐assemble in aqueous solution into discrete bundles of unique structure and defined stoichiometry. The first β‐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 β‐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 β‐peptide assemblies with defined sizes, reproducible structures, and sophisticated function.