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 D. Hamilton; Ernest Giralt

doi:10.1021/ja9910154

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 D. Hamilton, Ernest Giralt

Chemistry

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	11813-11820
Number of pages	8
Journal	Journal of the American Chemical Society
Volume	121
Issue number	50
DOIs	https://doi.org/10.1021/ja9910154
State	Published - Dec 22 1999

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

Access to Document

10.1021/ja9910154

Cite this

@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 Hamilton, {Andrew D.} and Ernest Giralt",

year = "1999",

month = dec,

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 D.

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

AN - SCOPUS:0033596316

SN - 0002-7863

VL - 121

SP - 11813

EP - 11820

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 50

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this