title: In Vitro Elucidation of the Folding Intermediates and Aggregate Formation of Hemoglobin Induced by Acetonitrile: A Multispectroscopic Approach.
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.
authors: Mohammad
authors: M
authors: Furkan
authors: Asim
authors: A
authors: Rizvi
authors: Mohammad
authors: M
authors: Afsar
authors: Mohammad Rehan
authors: MR
authors: Ajmal
authors: Rizwan H
authors: RH
authors: Khan
authors: Department of Biochemistry, Faculty of Life Science, Aligarh Muslim University, Aligarh, 202002 India. anaeem.bc@amu.ac.in.
authors: Aabgeena
authors: A
authors: Naeem
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006454:Hemoglobins / Q000737:chemistry*; D066298:In Vitro Techniques; D046529:Microscopy, Electron, Transmission; D062105:Molecular Docking Simulation; D017510:Protein Folding; D013056:Spectrophotometry, Ultraviolet; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D006454:Hemoglobins