Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor

Thomas Haack, Mark W. Peczuh, Xavier Salvatella, Jorge Sánchez-Quesada, Javier De Mendoza, Andrew Hamilton, Ernest Giralt

Research output: Contribution to journalArticle

Abstract

The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) 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.

Original languageEnglish (US)
Pages (from-to)11813-11820
Number of pages8
JournalJournal of the American Chemical Society
Volume121
Issue number50
DOIs
StatePublished - Dec 22 1999

Fingerprint

Artificial Receptors
Static Electricity
Peptides
Electrostatics
Stabilization
Guanidine
Hydrogen Bonding
Coulomb interactions
Nuclear magnetic resonance spectroscopy
Methanol
Conformations
Hydrogen bonds
Magnetic Resonance Spectroscopy
Topology
Water
Chemical analysis
Experiments

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor. / Haack, Thomas; Peczuh, Mark W.; Salvatella, Xavier; Sánchez-Quesada, Jorge; De Mendoza, Javier; Hamilton, Andrew; Giralt, Ernest.

In: Journal of the American Chemical Society, Vol. 121, No. 50, 22.12.1999, p. 11813-11820.

Research output: Contribution to journalArticle

Haack, Thomas ; Peczuh, Mark W. ; Salvatella, Xavier ; Sánchez-Quesada, Jorge ; De Mendoza, Javier ; Hamilton, Andrew ; Giralt, Ernest. / Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor. In: Journal of the American Chemical Society. 1999 ; Vol. 121, No. 50. pp. 11813-11820.
@article{f43daae55bcc493cbfcc6bcdbfd000be,
title = "Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor",
abstract = "The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10{\%} H2O/90{\%} CH3OH) 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.",
author = "Thomas Haack and Peczuh, {Mark W.} and Xavier Salvatella and Jorge S{\'a}nchez-Quesada and {De Mendoza}, Javier and Andrew Hamilton and Ernest Giralt",
year = "1999",
month = "12",
day = "22",
doi = "10.1021/ja9910154",
language = "English (US)",
volume = "121",
pages = "11813--11820",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "50",

}

TY - JOUR

T1 - Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor

AU - Haack, Thomas

AU - Peczuh, Mark W.

AU - Salvatella, Xavier

AU - Sánchez-Quesada, Jorge

AU - De Mendoza, Javier

AU - Hamilton, Andrew

AU - Giralt, Ernest

PY - 1999/12/22

Y1 - 1999/12/22

N2 - The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) 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.

AB - The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) 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.

UR - http://www.scopus.com/inward/record.url?scp=0033596316&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033596316&partnerID=8YFLogxK

U2 - 10.1021/ja9910154

DO - 10.1021/ja9910154

M3 - Article

VL - 121

SP - 11813

EP - 11820

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 50

ER -