The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion.
Recent studies suggest the dominant role of main-chain H-bond formation in specifying beta-sheet topology. Its essentially sequence-independent nature implies a large degree of freedom in designing beta-sheet-based nanomaterials. Here we show rational design of beta-sheet face inversions by incremental deletions of beta-strands from the single-layer beta-sheet of Borrelia outer surface protein A. We show that a beta-sheet structure can be maintained when a large number of native contacts are removed and that one can design large-scale conformational transitions of a beta-sheet such as face inversion by exploiting the promiscuity of strand-strand interactions. High-resolution X-ray crystal structures confirmed the success of the design and supported the importance of main-chain H-bonds in determining beta-sheet topology. This work suggests a simple but effective strategy for designing and controlling nanomaterials based on beta-rich peptide self-assemblies.
Makabe
Koki
K
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.
Koide
Shohei
S
D000595:Amino Acid Sequence; D000942:Antigens, Bacterial / Q000737:chemistry*; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D017122:Bacteriophage T4 / Q000201:enzymology; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D010446:Peptide Fragments; C077030:OspB protein, Borrelia burgdorferi; D009113:Muramidase