PMID: 7030403Nov 30, 1981Paper

Proton NMR investigation of Ln3+ complexes of thymopoietin 32-36

Biochimica Et Biophysica Acta
J B VaughnG Goldstein

Abstract

The pentapeptide Arg-Lys-Asp-Val-Tyr (TP5) is a biologically active fragment of thymopoietin, the thymic hormone that induces selective T-cell differentiation. The formation of lanthanide(III) complexes of TP5 is demonstrated through the observation of Tb3+ fluorescence enhancement. The equilibria, stoichiometry and solution conformation of the La3+, Pr3+ and Yb3+ complexes of TP5 have been investigated using NMR spectroscopy. In addition, the dissociation constants of two methyl ester analogs of TP5 have been studied. Evidence is presented supporting an interaction between the arginine guanidino N epsilon H and the aspartate carboxylate of TP5. Binding of Ln3+ appears to be accompanied by a disruption (or weakening) of this interaction and a concomitant increase in the 180 degrees rotamer population for the aspartate carboxylate group. The observed trends in the magnitudes of the dissociation constants and the rotamer populations appear to suggest that, although a significant amount of monodentate complexes may also exist, the metal ion binds predominantly to both carboxylates in a bidentate fashion.

References

Oct 12, 1979·Biochemical and Biophysical Research Communications·P H NaylorA L Goldstein
Dec 8, 1976·Journal of the American Chemical Society·H G BrittainR B Martin
Aug 1, 1975·Cell·D H Schlesinger, G Goldstein
Dec 31, 1973·Annals of the New York Academy of Sciences·I D CampbellA V Xavier
Apr 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·R S Basch, G Goldstein

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Citations

Jan 1, 1991·Molecular Immunology·Z WieczorekI Z Siemion
Jan 1, 1984·International Journal of Peptide and Protein Research·D TourwéG Van Binst
Jul 7, 2021·Materials Science & Engineering. C, Materials for Biological Applications·Rui YuCongmei Chen

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