Publication | Closed Access
Single amino acid based self-assembled structure
92
Citations
18
References
2013
Year
Amino AcidsProtein AssemblyMolecular Self-assemblyPeptide ScienceAnalytical UltracentrifugationElectron MicroscopyProtein FoldingBiophysicsSingle Amino AcidsProtein ChemistryBiochemistryConformational StudyMacromolecular ArchitectureMolecular ModelingHierarchical AssemblyStructural BiologySingle Amino AcidNatural SciencesSelf-assemblyMacromolecular SystemPeptide SynthesisMolecular BiophysicsMedicine
Single amino acids (phenylalanine, tyrosine and glycine) have been evaluated for fibrillar structure under neutral, aqueous conditions using scanning electron microscopy, transmission electron microscopy, circular dichroism, FTIR, and Congo red and thioflavin T histological dye assays. All these techniques prove that aromatic amino acids, such as phenylalanine and tyrosine, do in fact form distinct fibrillar structures albeit without any secondary structural characteristics such as an α-helix or a β-sheet. The nature of the interactions between neighbouring amino acids in the fibrillar structures are purported to simply be non-covalent π–π interactions.
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