title: Unraveling the interaction of hemoglobin with a biocompatible and cleavable oxy-diester-functionalized gemini surfactant.
abstract: Surfactant-protein mixtures have attracted considerable research interest in recent years at the interface of chemical biology and medicinal chemistry. Herein, the interaction between a green gemini surfactant (C16-E2O-C16) and a redox protein hemoglobin was examined through a series of in vitro experimental techniques with an attempt to provide a comprehensive knowledge of the surfactant-protein binding interactions. Quantitative appraisal of the fluorescence/CV data showed that the binding of C16-E2O-C16to Hb leads to the formation of thermodynamically favorable non-covalent adduct with 1:1 stoichiometry. UV-vis spectra demonstrated that the effect of C16-E2O-C16on Hb is highly concentration dependent. Far-UV and near-UV CD spectra together elucidated the formation of molten globule state of Hb upon C16-E2O-C16addition. Temperature dependent CD explicated the effect of C16-E2O-C16on the thermal stability of Hb. Furthermore, the structural investigation of Hb via pyrene/synchronous/three-dimensional fluorescence and FT-IR spectroscopy provided the complementary information related to its microenvironmental and conformational changes. Computational studies delineated that C16-E2O-C16binds in the vicinity of β-37 Trp at the α1β2interface of Hb. Overall, this study is expected to clarify the binding mechanism between Hb/other congeners and surfactant at the molecular level that are known to have immense potential in biomedical and industrial areas.
authors.affiliation: Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India. Electronic address: drmohdakram@rediffmail.com.
authors.forename: Mohd
authors.initials: M
authors.lastname: Akram
authors.affiliation: Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India.
authors.forename: Sana
authors.initials: S
authors.lastname: Anwar
authors.affiliation: Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India.
authors.forename: Imtiyaz Ahmad
authors.initials: IA
authors.lastname: Bhat
authors.affiliation: Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India.
authors.lastname: Kabir-Ud-Din
mesh_terms: D000818:Animals; D001672:Biocompatible Materials / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D002417:Cattle; D004952:Esters / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D010100:Oxygen / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation / Q000187:drug effects; D000644:Quaternary Ammonium Compounds / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013501:Surface-Active Agents / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology; D013696:Temperature
chemical_list: C000617554:2,2'-((oxybis(ethane-1,2-diyl))bis(oxy))bis(N-hexadecyl-N,N-dimethyl-2-oxoethanaminium); D001672:Biocompatible Materials; D004952:Esters; D006454:Hemoglobins; D000644:Quaternary Ammonium Compounds; D013501:Surface-Active Agents; D010100:Oxygen
keywords: Binding; Docking; Green oxy-diester-functionalized gemini surfactant