Abstract
Acetonitrile is a mild solvent, which induces β-sheet conformation in proteins. The global conformational changes in Hb in the presence of ACN were studied using intrinsic fluorescence experiments, acrylamide quenching, ANS fluorescence measurements, soret absorbance spectroscopy, fourier transform infrared spectroscopy, circular dichroism, thioflavin T and congo red assay. Molecular docking showed the binding of hydrophobic residues of Hb to ACN. Hb exists as a partially unfolded intermediate state at 30% v/v ACN. Hb aggregates were obtained at 60% v/v ACN concentration, which were further confirmed by transmission electron microscopy.
Keywords: Hemoglobin, acetonitrile, FTIR, CD, ANS, aggregates, TEM.
Graphical Abstract
Protein & Peptide Letters
Title:In Vitro Elucidation of the Folding Intermediates and Aggregate Formation of Hemoglobin Induced by Acetonitrile: A Multispectroscopic Approach
Volume: 23 Issue: 10
Author(s): Mohammad Furkan, Asim Rizvi, Mohammad Afsar, Mohammad Rehan Ajmal, Rizwan H. Khan and Aabgeena Naeem
Affiliation:
Keywords: Hemoglobin, acetonitrile, FTIR, CD, ANS, aggregates, TEM.
Abstract: Acetonitrile is a mild solvent, which induces β-sheet conformation in proteins. The global conformational changes in Hb in the presence of ACN were studied using intrinsic fluorescence experiments, acrylamide quenching, ANS fluorescence measurements, soret absorbance spectroscopy, fourier transform infrared spectroscopy, circular dichroism, thioflavin T and congo red assay. Molecular docking showed the binding of hydrophobic residues of Hb to ACN. Hb exists as a partially unfolded intermediate state at 30% v/v ACN. Hb aggregates were obtained at 60% v/v ACN concentration, which were further confirmed by transmission electron microscopy.
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Cite this article as:
Furkan Mohammad, Rizvi Asim, Afsar Mohammad, Ajmal Rehan Mohammad, Khan H. Rizwan and Naeem Aabgeena, In Vitro Elucidation of the Folding Intermediates and Aggregate Formation of Hemoglobin Induced by Acetonitrile: A Multispectroscopic Approach, Protein & Peptide Letters 2016; 23 (10) . https://dx.doi.org/10.2174/0929866523666160831154706
DOI https://dx.doi.org/10.2174/0929866523666160831154706 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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