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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 effects of side chains on peptide assembly,which are related to the assembly stability.