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The understanding of the driving force for peptide assembly is important,especially for the disease related amyloid aggregation.In this work,the assembly stability of model peptides(e.g.H5F5、F5H5、H5A5、A5H5、A5N5、N5A5、F5N5、N5F5、Y5F5、F5Y5、N5D5、D5N5)with different side chains has been studied by using STM(Scanning Tunneling Microscopy).The different length distributions reveal the sequence effects on peptide assembly,which are related to the assembly stability.We affirm the assembly stability of the peptides follows the order of Y > F > N > A > H,N > D.These works may provide new insights for understanding the structure of amyloid aggregates,the aggregation process and mechanism for inhibiting the amyloid aggregation.