Exploring the effect of surfactants on the interactions of manganese dioxide nanoparticles with biomolecules

AbstractInteractions of manganese dioxide nanoparticles (MnO2 NPs) with vital biomolecules namely deoxyribonucleic acid (DNA) and serum albumin (BSA) have been studied in association with different surfactants by using fluorescence (steady state, synchronous and 3D), UV-visible, resonance light scattering (RLS), dynamic light scattering (DLS), and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The esterase activity of serum albumin was tested in associations with MnO2 NPs and surfactants. The antioxidant potential of prepared NPs was also evaluated (DPPH method). Gel electrophoresis was carried out to analyze the effect of MnO2 NPs and surfactants on DNA. Presence of CTAB, Tween 20, DTAB and Tween 80 enhanced nanoparticle-protein binding. Tween 20 based nanoparticle systems showed long-term stability and biocompatibility. The quenching of BSA fluorescence emission in presence of MnO2 NPs alone and along with Tween 20 revealed stronger association of nanoparticles with proteins. Enhancement in the esterase activity (BSA) was observed in the presence of Tween 20. Furthermore, radical scavenging activity showed highest antioxidant potential in presence of Tween 20. The enthalpy and entropy assessment for protein-NPs association showed the predominance of Vander Waals interactions and hydrogen bonding. The synchronous fluorescence analysis highlighted the involvement of tryptophan (Trp) in the MnO2 NPs-protein interactions. The study evaluates the influence of surfactant on the associations of MnO2 NPs with the essential biomolecules. The findings can be crucially utilized in designing biocompatible MnO2 formulations for long term applications.Communicated by Ramaswamy H. SarmaHighlightsInfluence of conventional surfactants on MnO2 NPs- protein interactions.Tween 20 causes no harm to DNA and protein structures and delivers long-term biocompatibility.Static mode of quenching is observed for MnO2 NPs/Tween 20-protein systems.The thermodynamic analysis signifies the dominance of Vander Waals interactions and hydrogen bonding amongst MnO2 NPs/Tween 20 and BSA systems.The findings will aid in designing stable and biocompatible MnO2 NPs for future therapeutic application.Keywords: MnO2 NPsvital biomolecules (DNABSA)surfactantscysteine reactivityesterase activitythermodynamic factors AcknowledgmentsWe sincerely thank Malaviya National Institute of Technology Jaipur (Materials Research Centre) for SEM, EDX and elemental mapping studies. We also acknowledge SAIF, Panjab University for XRD analysis.Disclosure statementNo potential conflict of interest was reported by the author(s).Additional informationFundingThe author(s) reported there is no funding associated with the work featured in this article.Notes on contributorsShagufta KhanShagufta Khan (PhD Student): Participation in Conceptualization, Investigation, Methodology, Data curation, Formal analysis and Writing-original draft.Prairna BalyanPrairna Balyan (PhD Student): Participation in carrying out SDS-PAGE, Esterase activity, Cysteine reactivity, DPPH test and Interaction studies with DNA.Ahmad AliAhmad Ali: Supervision and editing of results related to SDS-PAGE, Esterase activity, Cysteine reactivity, DPPH test and Interaction analysis with DNA.Shweta SharmaShweta Sharma: Supervision and examination of nanoparticle characterization results.Shilpee SacharShilpee Sachar: Supervision (Principle investigator), Visualization, Writing- Reviewing and Editing.