NDLI: Toward an estimation of binding constants in aqueous solution: studies of associations of vancomycin group antibiotics.

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Molecular recognition

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Molecular recognition analyzed by docking simulations: the aspartate receptor and isocitrate dehydrogenase from Escherichia coli.

Design of a metallo-bZIP protein that discriminates between CRE and AP1 target sites: selection against AP1.

A genetic approach to the generation of antibodies with enhanced catalytic activities.

Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin.

Toward an estimation of binding constants in aqueous solution: studies of associations of vancomycin group antibiotics.

Energetics of cooperative binding of oligonucleotides with discrete dimerization domains to DNA by triple helix formation.

Anti-immune complex antibodies enhance affinity and specificity of primary antibodies.

Chemically bonded stationary phases that use synthetic hosts containing aromatic binding clefts: HPLC analysis of nitro-substituted polycyclic aromatic hydrocarbons.

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Recognition and catalysis in nucleic acid chemistry.

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Sequence conversion during postreplicative adenovirus overlap recombination.

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Characterization by yeast artificial chromosome cloning of the linked apolipoprotein(a) and plasminogen genes and identification of the apolipoprotein(a) 5′ flanking region

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Toward an estimation of binding constants in aqueous solution: studies of associations of vancomycin group antibiotics.

Content Provider	PubMed Central
Author	Williams, D. H. Searle, M. S. Mackay, J. P. Gerhard, U. Maplestone, R. A.
Abstract	An approach toward the estimation of binding constants for organic molecules in aqueous solution is presented, based upon a partitioning of the free energy of binding. Consideration is given to polar and hydrophobic contributions and to the entropic cost of rotor restrictions and bimolecular associations. Several parameters (derived from an analysis of entropy changes upon the melting of crystals and from the binding of cell wall peptide analogues to the antibiotic ristocetin A) which may be useful guides to a crude understanding of binding phenomena are presented: (i) amide-amide hydrogen bond strengths of -(1 to 7) +/- 2 kJ.mol-1, (ii) a hydrophobic effect of -0.2 +/- 0.05 kJ.mol-1.A-2 of hydrocarbon removed from exposure to water in the binding process, and (iii) free energy costs for rotor restrictions of 3.5-5.0 kJ.mol-1. The validity of the parameters for hydrogen bond strengths is dependent on the validity of the other two parameters. The phenomenon of entropy/enthalpy compensation is considered, with the conclusion that enthalpic barriers to dissociations will result in larger losses in translational and rotational entropy in the association step. The dimerization of some vancomycin group antibiotics is strongly exothermic (-36 to -51 kJ.mol-1) and is promoted by a factor of 50-100 by a disaccharide attached to ring 4 (in vancomycin and eremomycin) and by a factor of ca. 1000 by an amino-sugar attached to the benzylic position of ring 6 in eremomycin. The dimerization process (which, as required for an exothermic association, appears to be costly in entropy) may be relevant to the mode of action of the antibiotics.
Starting Page	1172
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	90
Language	English
Publisher Date	1993-02-15
Access Restriction	Open
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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