A5070286116- X-ray Diffraction in Crystallography
- Crystallization and Solubility Studies
- Chemical Synthesis and Analysis
- Supramolecular Self-Assembly in Materials
- Diatoms and Algae Research
- Advanced biosensing and bioanalysis techniques
- Metal-Organic Frameworks: Synthesis and Applications
- Molecular Junctions and Nanostructures
- Click Chemistry and Applications
- Supramolecular Chemistry and Complexes
The University of Tokyo
2023-2024
The steric zipper is a common hydrophobic packing structure of peptide side chains that forms between two adjacent β-sheet layers in amyloid and related fibrils. Although previous studies have revealed fragments derived from native protein sequences exhibit structures, their de novo designs rarely been studied. Herein, structures were artificially constructed the crystalline state by metal-induced folding assembly tetrapeptide Boc-3pa-X1-3pa-X2-OMe (3pa: β-(3-pyridyl)-l-alanine; X1 X2: amino...
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 four‐stranded anti‐parallel by utilizing non‐covalent approach. This was achieved folding and Ag + pentapeptide ( 1 ) Ala‐ D 3pa‐Gly‐3pa‐Val (3pa: β‐(3‐pyridyl)‐alanine) sequence, which designed form an interlocking 2 ring through metal cross‐linking side chains. NMR analyses X‐ray...
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 four‐stranded anti‐parallel by utilizing non‐covalent approach. This was achieved folding and Ag + pentapeptide ( 1 ) Ala‐ D 3pa‐Gly‐3pa‐Val (3pa: β‐(3‐pyridyl)‐alanine) sequence, which designed form an interlocking 2 ring through metal cross‐linking side chains. NMR analyses X‐ray...