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Publication Abstract from PubMed

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.

The promiscuity of beta-strand pairing allows for rational design of beta-sheet face inversion.,Makabe K, Koide S J Am Chem Soc. 2008 Nov 5;130(44):14370-1. Epub 2008 Oct 9. PMID:18842042^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.