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Research Articles

Exploring the structural basis of conformational alterations of myoglobin in the presence of spermine through computational modeling, molecular dynamics simulations, and spectroscopy methods

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Pages 3581-3594 | Received 06 Aug 2020, Accepted 04 Nov 2020, Published online: 14 Dec 2020
 

Abstract

Spermine as polyamines can have interaction with the myoglobin (Mb). The intent of this pondering to evaluate the impact of spermine on Mb properties, for example, the structure and thermal stability. For this analysis, the following approaches are employed. Thermodynamics, molecular dynamics (MD), and docking and the use of other spectroscopic procedures. The results of fluorescence spectroscopy and docking showed that binding spermine to Mb was spontaneous. Spermine quenched the fluorescence of Mb through the static quenching process. The thermal stability of Mb was incremented when the concentration of spermine increased. The CD spectra showed Mb’s secondary structure shift with a rise in β-sheet and a decrease in α-helicity Mb’s in spermine presence. Molecular docking and MD simulation outcomes demonstrate that electrostatic forces show a critical function in stabilizing of this complex, which is in conforming to spectroscopic results.

Communicated by Ramaswamy H. Sarma

Disclosure statement

No potential conflict of interest was reported by the authors.

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