ArticleProceedings of the National Academy of Sciences of the United States of America2012
Kinetics and thermodynamics of binding reactions as exemplified by anthrax toxin channel blockage with a cationic cyclodextrin derivative.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
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- Dynorphin A induces membrane permeabilization by formation of proteolipidic pores. Insights from electrophysiology and computational simulations.Computational and structural biotechnology journal · 2022Article
- VDAC Gating Thermodynamics, but Not Gating Kinetics, Are Virtually Temperature Independent.Biophysical journal · 2020Article
- Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catecholProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Lipid nanodomains change ion channel function.Nanoscale · 2017Article
- Inhibiting bacterial toxins by channel blockage.Pathogens and disease · 2016Review
- Lognormal distribution of firing time and rate from a single neuron?Cognitive neurodynamics · 2015Article
- Review
- Forces and dynamics of glucose and inhibitor binding to sodium glucose co-transporter SGLT1 studied by single molecule force spectroscopy.The Journal of biological chemistry · 2014Article
- Tailored cyclodextrin pore blocker protects mammalian cells from clostridium difficile binary toxin CDT.Toxins · 2014Article
- Stochastic detection of Pim protein kinases reveals electrostatically enhanced association of a peptide substrate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cyclodextrin derivatives as anti-infectives.Current opinion in pharmacology · 2013Review
- Single-molecule interrogation of a bacterial sugar transporter allows the discovery of an extracellular inhibitor.Nature chemistry · 2013Article
- The role of allosteric coupling on thermal activation of thermo-TRP channels.Biophysical journal · 2013Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
The thermodynamics of binding reactions is usually studied in the framework of the linear van't Hoff analysis of the temperature dependence of the equilibrium constant. The logarithm of the equilibrium constant is plotted versus inverse temperature to discriminate between two terms: an enthalpic contribution that is linear in the inverse temperature, and a temperature-independent entropic contribution. When we apply this approach to a particular case-blockage of the anthrax PA(63) channel by a multicharged cyclodextrin derivative-we obtain a nearly linear behavior with a slope that is characterized by enthalpy of about 1 kcal/mol. In contrast, from blocker partitioning between the channel and the bulk, we estimate the depth of the potential well for the blocker in the channel to be at least 8 kcal/mol. To understand this apparent discrepancy, we use a simple model of particle interaction with the channel and show that this significant difference between the two estimates is due to the temperature dependence of the physical forces between the blocker and the channel. In particular, we demonstrate that if the major component of blocker-channel interaction is van der Waals interactions and/or Coulomb forces in water, the van't Hoff enthalpy of the binding reaction may be close to zero or even negative, including cases of relatively strong binding. The results are quite general and, therefore, of importance for studies of enzymatic reactions, rational drug design, small-molecule binding to proteins, protein-protein interactions, and protein folding, among others.
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