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The Study On Solid Phase Organic Synthetic And Template-assisted Self-bassembly Of Peptides

Posted on:2019-10-26Degree:MasterType:Thesis
Country:ChinaCandidate:N LiFull Text:PDF
GTID:2370330566991185Subject:Biochemistry and Molecular Biology
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In recent years,self-assembly of biomolecules has become a hot research topic in the field of nanomaterials science.The self-assembly of DNA and peptide molecules has become the focus of many scholars.Peptide fibrillization is a self-assembly process which is a common phenomenon in living organisms.Understanding fibrillization of amyloid and the sequence of the core peptides is therefore of great significance in exploring nanobiological medicine.By designing and synthesizing peptides with different amino acid sequences,self-assembly can form a variety of nanostructures.These nanostructures have played an increasingly important role in the fields of materials science,nanobiomedicine and other fields.In this paper,the real-time method of atomic force microscope was used to deeply study the effect of concentration on the self-assembly process of pentapeptide?NH2-FFVLK-CONH2?on the surface of highly oriented pyrolytic graphite?HOPG?.And molecular dynamics simulation results provide more details for experimental.In the first part of this paper,the effect of concentration on the self-assembly of pentapeptide?P5?was studied.The results showed that:1)the speed of P5 self-assembly into a fiber structure is related to the concentration;The concentration determines the fiber height and the epitaxial growth on HOPG.The growth in length of the fiber is independent of the concentration.2)due to the?-?interacions between the phenyl groups in Phe residue and the hydrophobic graphite surface,P5 forms a double-layer,antiparallel?-sheet nanostructure on the surface of HOPG.The second part of this thesis mainly uses molecular dynamics simulation to construct a hydrophobic HOPG and pentapeptide model,which simulates the process of self-assembly of P5 on the surface of HOPG to form a nanofiber structure,indicating that only when P5 forms a double-layer,antiparallel?-sheet,the layer configuration is the most stable.The MD simulation results agree well with observations by the real-time atom force microscopy.Template Assisted Self Assembly?TASA?of Polypeptides on Inorganic Substrate Materials provides a basic understanding of the assisted self-assembly of polypeptide templates including the effect of hydrophobic interfaces on polypeptide fibrosis.These results provide new ideas for the self-assembly of peptides,which helps to further design nanostructures with medical value.
Keywords/Search Tags:Peptide, Template assisted self assembly, Nanofilament, Real-time atomic force microscopy, Molecular dynamics simulation
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