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Updated: Jun 9, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
A Discrete Four-Stranded β-Sheet through Catenation of M2L2 Metal-Peptide Rings
Eisuke Tsunekawa1, Makoto Fujita2,3,1, Tomohisa Sawada4,5,6
1Department of Applied Chemistry, School of Engineering, The University of Tokyo Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.
Abstract:
Methods for precisely constructing a β-sheet assembly with number-defined strands in solution remains quite limited due to its intense aggregation property. Here, we report the precise construction of a four-stranded anti-parallel β-sheet by utilizing a non-covalent approach. This was achieved by folding and assembly of Ag+ and a pentapeptide (1) with the Ala-D3pa-Gly-3pa-Val (3pa: β-(3-pyridyl)-alanine) sequence, which was designed to form an interlocking Ag2(1)2 ring through metal cross-linking of the side chains. NMR analyses and X-ray crystallographic studies characterized the structure of the discrete β-sheet assembly as well as the remarkable structural selectivity in terms of strands' number, orientation and the sheet type.
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