title: Temperature dependent rapid annealing effect induces amorphous aggregation of human serum albumin.
abstract: This study represents an analysis of the thermal aggregation of human serum albumin (HSA) induced by novel rosin modified compounds. The aggregation process causes conformational alterations in the secondary and tertiary structures of the proteins. The conversion of globular protein to amorphous aggregates was carried out by spectroscopic, calorimetric and microscopic techniques to investigate the factors that are responsible for the structural, conformational and morphological alteration in the protein. Our outcome results show that the aggregation of HSA was dependent on the hydrophobicity, charge and temperature, because the formation of amorphous aggregates occurs in the presence of a novel cationic rosin compound, quaternary amine of rosin diethylaminoethyl ester (QRMAE), at 40°C and pH 7.4 (but at 25°C on similar pH value, there was no evidence of aggregate formation). In addition, the parent compound of QRMAE, i.e., abietic acid, and other derivatives such as nonionic rosin compounds [(RMPEG-750) and (RMA-MPEG-750)] do not shows the aggregating property. This work provides precise and necessary information that aid in the understanding the effects of rosin derivative compounds on HSA. This study also restrains important information for athletes, health providers, pharmaceutical companies, industries, and soft drink-processing companies.
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
authors.forename: Mohd
authors.initials: M
authors.lastname: Ishtikhar
authors.affiliation: Surfactant Research Chair, Department of Chemistry, King Saud University, College of Science, P.O. Box-2455, Riyadh 11451, Saudi Arabia.
authors.forename: Mohd Sajid
authors.initials: MS
authors.lastname: Ali
authors.affiliation: Surfactant Research Chair, Department of Chemistry, King Saud University, College of Science, P.O. Box-2455, Riyadh 11451, Saudi Arabia.
authors.forename: Ayman M
authors.initials: AM
authors.lastname: Atta
authors.affiliation: Surfactant Research Chair, Department of Chemistry, King Saud University, College of Science, P.O. Box-2455, Riyadh 11451, Saudi Arabia.
authors.forename: Hammad
authors.initials: H
authors.lastname: Al-Lohedan
authors.affiliation: Laboratory of Immunology and Molecular Physiology, Zoology Department, Faculty of Science, Assiut University, Assiut 71516, Egypt.
authors.forename: Gamal
authors.initials: G
authors.lastname: Badr
authors.affiliation: Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India. Electronic address: rizwanhkhan@hotmail.com.
authors.forename: Rizwan Hasan
authors.initials: RH
authors.lastname: Khan
mesh_terms: D002151:Calorimetry; D002942:Circular Dichroism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D066329:Protein Aggregates; D011485:Protein Binding; D011487:Protein Conformation; D055550:Protein Stability; D012709:Serum Albumin / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013501:Surface-Active Agents / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics
chemical_list: D066329:Protein Aggregates; D012709:Serum Albumin; D013501:Surface-Active Agents
keywords: Amorphous aggregate; Athlete's health; Human serum albumin; Rosin-modified surfactants; Thermal aggregation