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Odd‐Even Sequence Effect of Surface‐Mediated Peptide Assemblies Observed by Scanning Tunneling Microscopy
Author(s) -
Guo Yuanyuan,
Wang Chenxuan,
Hou Jingfei,
Yang Aihua,
Zhang Xuemei,
Wang Yibing,
Zhang Min,
Yang Yanlian,
Wang Chen
Publication year - 2012
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201200656
Subject(s) - peptide , chemistry , scanning tunneling microscope , residue (chemistry) , sequence (biology) , crystallography , biophysics , self assembly , nanotechnology , biochemistry , organic chemistry , materials science , biology
The peptide assembly structures of polyglutamine (PolyQ) have been studied by using scanning tunneling microscopy (STM) with high spatial resolution in ambient conditions. 4,4′‐Bipyridyl (4Bpy) was introduced into the PolyQ 7 and PolyQ 8 peptide assemblies for labeling the C‐termini of the peptides. The fine structures of the 4Bpy‐PolyQ 7 and 4Bpy‐PolyQ 8 co‐assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ 7 and PolyQ 8 . One predominant apparent peptide strand length is observed for PolyQ 7 reflecting one predominant peptide conformation in assembly structures, while three major apparent strand lengths can be identified with PolyQ 8 reflecting three co‐existing peptide conformations in peptide assemblies. Such drastic difference in assembling characteristics can be considered as a reflection of asymmetric adsorption effect of peptides relating to odd‐even residue numbers of PolyQ 7 and PolyQ 8 .