Understanding the inuence of nanoparticles on the formation of protein amyloid brillation is cru-cial to extend their application in related biological diagnosis and nanomedicines.In this work,Ra-man spectroscopy was ...Understanding the inuence of nanoparticles on the formation of protein amyloid brillation is cru-cial to extend their application in related biological diagnosis and nanomedicines.In this work,Ra-man spectroscopy was used to probe the amyloid brillation of hen egg-white lysozyme in the pres-ence of silver nanoparticles(Ag-NPs)at di erent concentrations,combined with atomic force mi-croscopy and thioavin T(ThT)uorescence assays.Four representative Raman indicators were utilized to monitor transformation of the protein tertiary and secondary structures at the molecular level:the Trp doublet bands at 1340 and 1360 cm^(-1),the disul de stretching vibrational peak at 507 cm^(-1),the N-Cα-C stretching vibration at 933 cm^(-1),and the amide I band.All experimental results con rmed the concentration-dependent inuence of AgNPs on the hen egg-white lysozyme amyloid brillation kinetics.In the presence of AgNPs at low concentration(17μg/mL),electrostatic interaction of the nanoparticles stabilizes disul de bonds,and protects the Trp residues from exposure to hydrophilic environment,thus leading to formation of amorphous aggregates rather than brils.However,with the action of AgNPs at high concentration(1700μg/mL),the native disul de bonds of hen egg-white lysozyme are broken to form Ag-S bonds owing to the competition of electrostatic interaction from a great deal of nanoparticles.As for providing functional surfaces for protein to interact with,AgNPs play a bridge role in direct transformation from-helices to organized-sheets.The present investigation sheds light on the controversial e ects of AgNPs on the kinetics of hen egg-white lysozyme amyloid brillation.展开更多
基金This work was supported by the National Natu-ral Science Foundation of China(No.22073088 and No.21873089).
文摘Understanding the inuence of nanoparticles on the formation of protein amyloid brillation is cru-cial to extend their application in related biological diagnosis and nanomedicines.In this work,Ra-man spectroscopy was used to probe the amyloid brillation of hen egg-white lysozyme in the pres-ence of silver nanoparticles(Ag-NPs)at di erent concentrations,combined with atomic force mi-croscopy and thioavin T(ThT)uorescence assays.Four representative Raman indicators were utilized to monitor transformation of the protein tertiary and secondary structures at the molecular level:the Trp doublet bands at 1340 and 1360 cm^(-1),the disul de stretching vibrational peak at 507 cm^(-1),the N-Cα-C stretching vibration at 933 cm^(-1),and the amide I band.All experimental results con rmed the concentration-dependent inuence of AgNPs on the hen egg-white lysozyme amyloid brillation kinetics.In the presence of AgNPs at low concentration(17μg/mL),electrostatic interaction of the nanoparticles stabilizes disul de bonds,and protects the Trp residues from exposure to hydrophilic environment,thus leading to formation of amorphous aggregates rather than brils.However,with the action of AgNPs at high concentration(1700μg/mL),the native disul de bonds of hen egg-white lysozyme are broken to form Ag-S bonds owing to the competition of electrostatic interaction from a great deal of nanoparticles.As for providing functional surfaces for protein to interact with,AgNPs play a bridge role in direct transformation from-helices to organized-sheets.The present investigation sheds light on the controversial e ects of AgNPs on the kinetics of hen egg-white lysozyme amyloid brillation.
