December 1, 1999Journal of the American Chemical Society

Surface Recognition and Helix Stabilization of a Tetraaspartate Peptide by Shape and Electrostatic Complementarity of an Artificial Receptor

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Authors

THThomas HaackUniversitat de Barcelona MPMark W. PeczuhHarvard University XSXavier SalvatellaInstitució Catalana de Recerca i Estudis Avançats

Abstract

The recognition of tetraaspartate peptide ( 2 ) by tetra-guanidinium ( 1 ) in (a) water and (b) aqueous methanol (10% H 2 O/90% CH 3 OH) has been investigated. The conformations of the free peptide and its complex with 1 have been characterized in both solvent systems by CD and 2D NMR spectroscopies. Increased α-helicity as a result of solvent composition and receptor binding are discussed. Control experiments show that the recognition stems from complementary electrostatic interactions, hydrogen bonding, and matching of surface topologies.

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Haack et al. (1999) studied this question.

synapsesocial.com/papers/6a7aa62a14b028facf0e79c8 https://doi.org/10.1021/ja9910154

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Surface Recognition and Helix Stabilization of a Tetraaspartate Peptide by Shape and Electrostatic Complementarity of an Artificial Receptor

Abstract

Discussion

Cite This Study

Surface Recognition and Helix Stabilization of a Tetraaspartate Peptide by Shape and Electrostatic Complementarity of an Artificial Receptor

Abstract

Discussion

Cite This Study

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