Peptides and proteins are known to form a variety of ordered structures via assembling processes. The molecular insights of the assembly propensities of various peptide-based nanostructures are keen to the pharmaceutical studies and pathological analysis for neurodegenerative disorder processes such as Alzheimer’s disease (AD). Documented experimental results have revealed that the capability of peptides to form ordered structures has significant dependence on the sequence and composition of amino acids. An important subject under study is the formation mechanisms of peptide assemblies at the level of individual amino acids. We have endeavored to investigate the assembly propensity of peptides based on the high resolution structural analysis of surface-bound peptide assemblies by using scanning tunneling microscopy (STM). Specifically, the dependence of the peptide assembly structures on sequences will be pursued, including the impact of amino acids on the adsorption stability and assembly propensity. It may be anticipated that these efforts could advance the fundamental mechanism underlying the peptide assembly propensity, as well as provide the potential venues for developing novel diagnosis and therapeutic approaches towards relevant diseases.

Molecular mechanism of peptide assembly propensity studied with STM

2019 Spring National Meeting

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