title: Effect of sucrose on chemically and thermally induced unfolding of domain-I of human serum albumin: Solvation dynamics and fluorescence anisotropy study.
abstract: The present study is devoted to understand the effect of sucrose on the hydration dynamics and rotational relaxation dynamics within the domain-I of HSA during chemically as well as thermally induced unfolding. It has been observed that the average solvation time become slower in the presence of sucrose for the lower concentrations of GnHCl, however at higher concentrations of GnHCl the effect of sucrose is almost negligible. From the time resolved fluorescence anisotropy it has been observed that in the lower concentration region of GnHCl the sucrose induced stabilization is small as compared to the higher concentrations of GnHCl. We have concluded that the hydration dynamics plays an important role in the sucrose induced stabilization process at the low concentration region; whereas environmental restriction is responsible at the higher concentration of GnHCl. However, we have observed a negligible stabilizing effect of sucrose towards the temperature induced unfolding.
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur, 208 016, UP, India.
authors.forename: Rajeev
authors.initials: R
authors.lastname: Yadav
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur, 208 016, UP, India.
authors.forename: Bhaswati
authors.initials: B
authors.lastname: Sengupta
authors.affiliation: Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur, 208 016, UP, India. Electronic address: psen@iitk.ac.in.
authors.forename: Pratik
authors.initials: P
authors.lastname: Sen
mesh_terms: D005454:Fluorescence Polarization; D006801:Humans; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D012709:Serum Albumin / Q000737:chemistry*; D012995:Solubility; D013050:Spectrometry, Fluorescence; D013395:Sucrose / Q000737:chemistry*; D013696:Temperature
chemical_list: D012709:Serum Albumin; D013395:Sucrose
keywords: Chemical denaturation; Fluorescence anisotropy; Human serum albumin; Solvation dynamics; Stabilization; Sucrose; Thermal denaturation