Issue 15, 2000

Side chain elongation causes a change from enthalpy driven to entropy driven binding in the molecular recognition of tetraanionic peptidesElectronic supplementary information (ESI) available: isothermal titration calorimetry, 1HNMR and NOE data. See http://www.rsc.org/suppdata/cc/b0/b003728l/

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.

Supplementary files

Article information

Article type
Communication
Submitted
10 May 2000
Accepted
21 Jun 2000
First published
07 Jul 2000

Chem. Commun., 2000, 1399-1400

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

X. Salvatella, M. W. Peczuh, M. Gairí, R. K. Jain, J. Sánchez-Quesada, J. de Mendoza, A. D. Hamilton and E. Giralt, Chem. Commun., 2000, 1399 DOI: 10.1039/B003728L

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