De Novo Protein Surface Design: Use of Cation-π Interactions to Enhance Binding between an α-Helical Peptide and a Cationic Molecule in 50 % Aqueous Solution
- 2 January 2002
- journal article
- review article
- Published by Wiley in Angewandte Chemie International Edition in English
- Vol. 41 (1) , 117-119
- https://doi.org/10.1002/1521-3773(20020104)41:1<117::aid-anie117>3.0.co;2-j
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Polar Interactions with Aromatic Side Chains in α-Helical Peptides: Ch···O H-Bonding and Cation−π InteractionsJournal of the American Chemical Society, 2001
- The Role of Cation−π Interactions in Biomolecular Association. Design of Peptides Favoring Interactions between Cationic and Aromatic Amino Acid Side ChainsJournal of the American Chemical Society, 2001
- Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptidesChemical Communications, 2000
- Surface Recognition and Helix Stabilization of a Tetraaspartate Peptide by Shape and Electrostatic Complementarity of an Artificial ReceptorJournal of the American Chemical Society, 1999
- Recognition and Stabilization of an α-Helical Peptide by a Synthetic ReceptorJournal of the American Chemical Society, 1997
- Design, synthesis and evaluation of synthetic receptors for the recognition of aspartate pairs in an α-helical conformationBioorganic & Medicinal Chemistry, 1997
- The Cation−π InteractionChemical Reviews, 1997
- Molecular Recognition of Proteins: Sequence-Selective Binding of Aspartate Pairs in Helical PeptidesJournal of the American Chemical Society, 1995
- Specific inhibition of flavin catalyses by a “molecular hinge”Tetrahedron Letters, 1989
- Induced fit in synthetic receptors: nucleotide base recognition by a molecular hingeJournal of the American Chemical Society, 1987