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Sphingomyelin-induced structural modification of native human hemoglobin and its chemically and thermally disrupted secondary structure: A photophysical exploration
R. Sett, S. Sen,
Published in Elsevier B.V.
PMID: 32146276
Volume: 190
Sphingomyelin-induced structural modification of Human Hemoglobin (Hb) has been investigated in its native and unfolded conformers that are partially denatured in presence of ∼ 4 M urea, completely denatured in ∼ 8 M urea and thermally disrupted (at ∼ 65 °C) state. The absorption studies unveil ground state complexation between Hb and SM. From steady-state fluorescence and quenching studies alteration of the micro-environments around Trp residues of Hb in above mentioned different cases has been determined. Moreover, lesser exposure of Trp residues to SM in thermally disrupted Hb can be accounted for the exceptionally interesting outcomes in other experiments. The alterations in the time-resolved decay profiles of native Hb, partially and totally chemically denatured as well as thermally disrupted Hb with gradual addition of SM also affirm the amendment of the proteinous micro-environment surrounding Trp residues in a view of FRET between Trp residues and heme group. Wavelength-sensitive emission spectral studies reveal that the protein shows red edge effect in its different conformations in presence and absence of SM. Interestingly, the wavelength-responsive time-resolved study at a constant excitation wavelength demonstrates that with addition of lipid the increment of the average fluorescence lifetime signifies a considerable modulation of solvation dynamics of the fluorescent Trp residues in their excited state being greatest in case of thermally disrupted Hb. Nevertheless, the loss of α-helicity of Hb at its various conformers with addition of SM has been portrayed thoroughly by means of far-UV CD spectral studies in a view of disruption of secondary structure of the protein. © 2020 Elsevier B.V.
About the journal
JournalData powered by TypesetColloids and Surfaces B: Biointerfaces
PublisherData powered by TypesetElsevier B.V.