Study On The Compusition,Structure And Mechanism Of Protein Corona

Nanomaterials are expected to be a versatile diagnostic and therapeutic tool.However,due to the limited understanding and control of the interaction of nanomaterials with complex biological systems,the effective application of nanomaterials is hindered.When a nanomaterial enters a physiological environment,it rapidly adsorbs proteins that form a “protein corona”.Protein corona alter the size and interfacial composition of nanomaterials,making them biologically different from synthetic materials.Biological properties determine physiological responses including signaling,kinetics,transport,accumulation,and toxicity.Therefore,the study of the properties of protein corona on nanomaterials is of great significance.Here,ultrasmall gold nanoparticles(AuNPs)coated by human serum albumin(HSA)corona were studied by Fourier transform infrared spectroscopy,denature experiment,fluorescence quenching.Moreover,the interacellular fate of AuNPs and the AuNP-HSA corona has also been investigated.The results show that HSA corona undergo a conformational transition(partial ?-sheet changed to ?-helicity)when they adsorb on AuNPs,which lead to an enhanced thermal stability.Importantly,we observed that the conformation-transited protein corona-AuNP complex could induce cell apoptosis.Meanwhile,for the first time,more attentions are paid to the conformation-transited-HSA-AuNPs adhere and damage cell membrane,which may induce to cell toxicity.The results obtained here not only provide the detailed conformational behavior of HSA molecules on nanoparticles,but also reveal the structure-function relationship of protein corona,which is of utmost importance in the safe application of nanoscale objects in living organisms.Magnetic iron oxide nanoparticles(MIONPs)have been intensely applied to bioapplications.In a physiological environment(e.g.,blood),Proteins will bind nanoparticles to shape a “protein corona” layer.The structure and aggregation of protein corona around the nanoparticles are important in the growing biosafety concern of nanomaterials.We present a systematic method,including transmission electron microscopy,energy dispersive X-ray spectroscopy,dynamic light scattering,Fourier transform infrared spectroscopy and hydrogen–deuterium exchange techniques,to explore the conformational change,thermal stability and aggregation of protein corona bound on magnetic iron oxide nanoparticles.We found that protein corona bound on MIONPs are partially unfolded at physiological environment.Furthermore,for the first time we observed that the morphology and the conformational change of the protein corona at the MIONPs surface can induce the protein aggregates.We believe that these findings will deepen our understanding of the protein corona,which is of utmost importance in the safe application of nanoscale objects in living organisms.Qualitative analysis of human serum albumin adsorbed on citrate-reduced gold nanoparticles(AuNPs)and silver nanoparticles(AgNPs)by gel electrophoresis combined with matrix-assisted laser desorption(sorption)ionization cascade time-of-flight mass spectrometry(MALDI-TOF)And quantitative analysis and identification analysis.We found that as the incubation time in human serum albumin increased,the serum albumin adsorbed on the two nanomaterials was gradually replaced by immune-related proteins,and we found that the adsorption of serum proteins by different nanomaterials at the same time.There are significant differences in rate and selectivity.This is important for immune safety,biocompatibility,and the development of novel nanomaterials that have important biological functions and are highly specific and selective for proteins.In this paper,the structural analysis of protein corona on ultra-small gold nanoparticles and magnetic iron oxide surface and the dynamic exchange of protein corona on the surface of precious metals were analyzed.These findings will guide the interaction between nanomaterials and biological interfaces and are critical for the safe use of nanoscale objects in vivo.