title: Acetonitrile can promote formation of different structural intermediate states on aggregation pathway of immunoglobulin G from human and bovine.
abstract: A sequential addition of acetonitrile to human and bovine immunoglobulin G induces molten globule-like state at 50% (v/v) and 60% (v/v) respectively having secondary structure similar to native protein as evident from far-UV circular dichroism and Fourier transform infra red spectroscopy. Further addition of acetonitrile up to 80% forms aggregate of IgG as confirmed by increase in thioflavin T, loss of signals in near-UV CD spectra, decrease in ANS and tryptophan fluorescence. Thus at high acetonitrile concentration, a relatively large amount of partially unfolded intermediates of IgG are present which result in aggregates formation.
authors: Department of Biochemistry, Faculty of Life Science, Aligarh Muslim University, Aligarh 202 002, India.
authors: Samreen
authors: S
authors: Amani
authors: Aabgeena
authors: A
authors: Naeem
mesh_terms: D000097:Acetonitriles / Q000378:metabolism*; D000818:Animals; D052160:Benzothiazoles; D002417:Cattle; D002942:Circular Dichroism; D005453:Fluorescence; D006801:Humans; D007074:Immunoglobulin G / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017550:Spectroscopy, Fourier Transform Infrared; D013844:Thiazoles
chemical_list: D000097:Acetonitriles; D052160:Benzothiazoles; D007074:Immunoglobulin G; D013844:Thiazoles; C009462:thioflavin T; C032159:acetonitrile