N-(tert-butoxycarbonyl)-L-valyl-L-valine methyl ester: a twisted parallel β-sheet in the crystal structure of a protected dipeptide.

Øyvind Jacobsen, Hadgu Girmay Gebreslasie, Jo Klaveness, Pål Rongved, Carl Henrik Görbitz

School of Pharmacy, University of Oslo, Oslo, Norway.

Acta crystallographica. Section C, Crystal structure communications 2011 Aug

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The title compound, C(16)H(30)N(2)O(5), crystallizes with three molecules in the asymmetric unit, each adopting a β-strand/polyproline II backbone conformation. The main-chain functional groups are hydrogen bonded into tapes having the characteristics of parallel β-sheets. Each tape has a left-handed twist and thus forms a helix, with six peptide molecules needed to complete a full 360° rotation. A comparison of hydrogen-bond lengths and twisting modes is made with other related structures of protected dipeptides and with a hexapeptide derived from amyloid-β containing the Val-Val segment. Additionally, a comparison of the backbone conformation is made with that of the Val141-Val142 segment of the water channel aquaporin-4 (AQP4).

Citation

Øyvind Jacobsen, Hadgu Girmay Gebreslasie, Jo Klaveness, Pål Rongved, Carl Henrik Görbitz. N-(tert-butoxycarbonyl)-L-valyl-L-valine methyl ester: a twisted parallel β-sheet in the crystal structure of a protected dipeptide. Acta crystallographica. Section C, Crystal structure communications. 2011 Aug;67(Pt 8):o278-82