PMID: 2125011Dec 10, 1990Paper

Electrostatic repulsion between molecules of like charge can be misinterpreted as binding

FEBS Letters
P Stemmer, C B Klee

Abstract

Spectroscopic methods have shown that Ca2+ chelators interact with Ca2(+)-binding proteins. These spectral alterations have been interpreted as evidence for the binding of chelator by the proteins. We show by direct examination of EDTA interaction with calmodulin and alpha-lactalbumin that these proteins repel EDTA rather than bind it. The repulsion is reduced by increased salt concentration but is unaffected by Ca2+ binding to the proteins. The acidic protein, alpha-lactalbumin, repells the negatively charged EDTA and inorganic phosphate whereas the basic protein, lysozyme, repells the positively charged spermine. Thus, spectroscopic changes induced by negatively charged Ca2+ chelators on negatively charged Ca2(+)-binding proteins are due to electrostatic repulsion, and not to binding. These observations underscore the possible pitfalls of using spectroscopic methods alone to analyze protein-ligand interactions.

References

Jan 1, 1989·Critical Reviews in Biochemistry and Molecular Biology·M J Kronman
Apr 8, 1987·Biochimica Et Biophysica Acta·J DesmetF van Cauwelaert
Sep 1, 1985·International Journal of Peptide and Protein Research·Y Hiraoka, S Sugai
Aug 1, 1984·Analytical Biochemistry·L Lindahl, H J Vogel
Aug 5, 1980·Biochemistry·T H Crouch, C B Klee
Oct 8, 1962·Biochimica Et Biophysica Acta·J P HUMMEL, W J DREYER

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