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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Research Article

In Vitro Elucidation of the Folding Intermediates and Aggregate Formation of Hemoglobin Induced by Acetonitrile: A Multispectroscopic Approach

Author(s): Mohammad Furkan, Asim Rizvi, Mohammad Afsar, Mohammad Rehan Ajmal, Rizwan H. Khan and Aabgeena Naeem

Volume 23, Issue 10, 2016

Page: [884 - 891] Pages: 8

DOI: 10.2174/0929866523666160831154706

Price: $65

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


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