期刊
BIOCHEMISTRY
卷 55, 期 23, 页码 3214-3223出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00201
关键词
-
资金
- Air Force Office of Scientific Research Grant [FA9550-14-1-0350]
The self-assembly of peptides and proteins into higher-ordered structures is encoded in the amino acid sequence of each peptide or protein. Understanding the relationship among the amino add sequence, the assembly dynamics, and the structure of well-defined peptide oligomers expands the synthetic toolbox for these structures. Here, we present the X-ray crystallographic structure and solution behavior of de novo peptides that form antiparallel coiled-coil hexamers (ACC-Hex) by an interaction motif neither found in nature nor predicted by existing peptide design software. The 1.70 angstrom X-ray crystallographic structure of peptide la shows six a helices associating in an antiparallel arrangement around a central axis comprising hydrophobic and aromatic residues. Size exclusion chromatography studies suggest that peptides 1 form stable oligomers in solution, and circular dichroism experiments show that peptides 1 are stable to relatively high temperatures. Small-angle X-ray scattering studies of the solution behavior of peptide la indicate an equilibrium of dimers, hexamers, and larger aggregates in solution. The structures presented here represent a new motif of biomolecular self-assembly not previously observed for de novo peptides and suggest supramolecular design principles for material scaffolds based on coiled-coil motifs containing aromatic residues.
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