Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptides

Xavier Salvatella; Mark W. Peczuh; Margarida Gairí; Rishi K. Jain; Jorge Sánchez-Quesada; Javier De Mendoza; Andrew D. Hamilton; Ernest Giralt

doi:10.1039/b003728l

Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptides

Xavier Salvatella, Mark W. Peczuh, Margarida Gairí, Rishi K. Jain, Jorge Sánchez-Quesada, Javier De Mendoza, Andrew D. Hamilton, Ernest Giralt

Chemistry

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

Abstract

In binding to tetraguanidinium compounds, the average side chain length of tetraanionic peptides determines the thermodynamics of binding, the degree of helix induction and the rigidity of the complex formed.

Original language	English (US)
Pages (from-to)	1399-1400
Number of pages	2
Journal	Chemical Communications
Issue number	15
DOIs	https://doi.org/10.1039/b003728l
State	Published - Aug 7 2000

ASJC Scopus subject areas

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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10.1039/b003728l

Cite this

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title = "Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptides",

abstract = "In binding to tetraguanidinium compounds, the average side chain length of tetraanionic peptides determines the thermodynamics of binding, the degree of helix induction and the rigidity of the complex formed.",

author = "Xavier Salvatella and Peczuh, {Mark W.} and Margarida Gair{\'i} and Jain, {Rishi K.} and Jorge S{\'a}nchez-Quesada and {De Mendoza}, Javier and Hamilton, {Andrew D.} and Ernest Giralt",

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month = aug,

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doi = "10.1039/b003728l",

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AU - Salvatella, Xavier

AU - Peczuh, Mark W.

AU - Gairí, Margarida

AU - Jain, Rishi K.

AU - Sánchez-Quesada, Jorge

AU - De Mendoza, Javier

AU - Hamilton, Andrew D.

AU - Giralt, Ernest

PY - 2000/8/7

Y1 - 2000/8/7

N2 - In binding to tetraguanidinium compounds, the average side chain length of tetraanionic peptides determines the thermodynamics of binding, the degree of helix induction and the rigidity of the complex formed.

AB - In binding to tetraguanidinium compounds, the average side chain length of tetraanionic peptides determines the thermodynamics of binding, the degree of helix induction and the rigidity of the complex formed.

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DO - 10.1039/b003728l

M3 - Article

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EP - 1400

JO - Chemical Communications

JF - Chemical Communications

IS - 15

ER -

Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptides

Abstract

ASJC Scopus subject areas

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