Bhowmik, Debipreeta and Kumar, Gopinatha Suresh (2017) A comparative spectroscopic and calorimetric investigation of the interaction of amsacrine with heme proteins, hemoglobin and myoglobin. In: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 35 (6). pp. 1260-1271.
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The binding of the anilido aminoacridine derivative amsacrine with the heme proteins, hemoglobin, and myoglobin, was characterized by various spectroscopic and calorimetric methods. The binding affinity to hemoglobin was (1.21 +/- .05) x 10(5) M-1, while that to myoglobin was three times higher (3.59 +/- .15) x 10(5) M-1. The temperature-dependent fluorescence study confirmed the formation of ground-state complexes with both the proteins. The stronger binding to myoglobin was confirmed from both spectroscopic and calorimetric studies. The binding was exothermic in both cases at the three temperatures studied, and was favored by both enthalpy and entropy changes. Circular dichroism results, three-dimensional (3D) and synchronous fluorescence studies confirmed that the binding of amsacrine significantly changed the secondary structure of hemoglobin, while the change in the secondary structure of myoglobin was much less. New insights, in terms of structural and energetic aspects of the interaction of amsacrine with the heme proteins, presented here may help in understanding the structure-activity relationship, therapeutic efficacy, and drug design aspects of acridines.
| Item Type: | Journal Article |
|---|---|
| Publication: | JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS |
| Additional Information: | Copy right for this article belongs to the TAYLOR & FRANCIS INC, 530 WALNUT STREET, STE 850, PHILADELPHIA, PA 19106 USA |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 25 May 2017 10:10 |
| Last Modified: | 25 May 2017 10:10 |
| URI: | http://eprints.iisc.ac.in/id/eprint/57074 |
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