Odd-Even Sequence Effect of Surface-Mediated Peptide Assemblies Observed by Scanning Tunneling Microscopy
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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C-termini of the peptides. T...
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| Published in | Chinese journal of chemistry Vol. 30; no. 9; pp. 1987 - 1991 |
|---|---|
| Main Author | |
| Format | Journal Article |
| Language | English |
| Published |
Weinheim
WILEY-VCH Verlag
01.09.2012
WILEY‐VCH Verlag Wiley Subscription Services, Inc |
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| ISSN | 1001-604X 1614-7065 |
| DOI | 10.1002/cjoc.201200656 |
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| Abstract | 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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C-termini of the peptides. The fine structures of the 4Bpy-PolyQ7 and 4Bpy-PolyQ8 co-assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ7 and PolyQs. One predominant apparent peptide strand length is ob- served for PolyQ7 reflecting one predominant peptide conformation in assembly structures, while three major ap- parent strand lengths can be identified with PolyQ8 reflecting three co-existing peptide conformations in peptide as- semblies. Such drastic difference in assembling characteristics can be considered as a reflection of asymmetric ad- sorption effect ofpeptides relating to odd-even residue numbers of PolyQ7 and PolyQ8, |
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| AbstractList | 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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C-termini of the peptides. The fine structures of the 4Bpy-PolyQ7 and 4Bpy-PolyQ8 co-assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ7 and PolyQs. One predominant apparent peptide strand length is ob- served for PolyQ7 reflecting one predominant peptide conformation in assembly structures, while three major ap- parent strand lengths can be identified with PolyQ8 reflecting three co-existing peptide conformations in peptide as- semblies. Such drastic difference in assembling characteristics can be considered as a reflection of asymmetric ad- sorption effect ofpeptides relating to odd-even residue numbers of PolyQ7 and PolyQ8, 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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C‐termini of the peptides. The fine structures of the 4Bpy‐PolyQ7 and 4Bpy‐PolyQ8 co‐assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ7 and PolyQ8. One predominant apparent peptide strand length is observed for PolyQ7 reflecting one predominant peptide conformation in assembly structures, while three major apparent strand lengths can be identified with PolyQ8 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 PolyQ7 and PolyQ8. Odd‐even effect is observed for assembly structures of PolyQ7 and PolyQ8 by STM, which could be associated with the adsorption conformations of the peptides. 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 . 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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C-termini of the peptides. The fine structures of the 4Bpy-PolyQ7 and 4Bpy-PolyQ8 co-assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ7 and PolyQ8. One predominant apparent peptide strand length is observed for PolyQ7 reflecting one predominant peptide conformation in assembly structures, while three major apparent strand lengths can be identified with PolyQ8 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 PolyQ7 and PolyQ8. |
| Author | Hou, Jingfei Yang, Yanlian Zhang, Xuemei Wang, Yibing Guo, Yuanyuan Wang, Chen Wang, Chenxuan Yang, Aihua Zhang, Min |
| AuthorAffiliation | National Center for Nanoseience and Technology, Beoing 100190, China |
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| Notes | peptide, adsorption, conformation, odd-even effect, scanning tunneling microscopy 31-1547/O6 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 PolyQ7 and PolyQ8 peptide assemblies for labeling the C-termini of the peptides. The fine structures of the 4Bpy-PolyQ7 and 4Bpy-PolyQ8 co-assemblies are observed, and the statistics of the apparent peptide strand length reveal different length distributions for PolyQ7 and PolyQs. One predominant apparent peptide strand length is ob- served for PolyQ7 reflecting one predominant peptide conformation in assembly structures, while three major ap- parent strand lengths can be identified with PolyQ8 reflecting three co-existing peptide conformations in peptide as- semblies. Such drastic difference in assembling characteristics can be considered as a reflection of asymmetric ad- sorption effect ofpeptides relating to odd-even residue numbers of PolyQ7 and PolyQ8 istex:478685DFE185BF013B17C567757FE1273484FF34 ArticleID:CJOC201200656 ark:/67375/WNG-Q128FGBB-W the National Basic Research Program of China - No. 2011CB932800, 2009CB930100 the Chinese Academy of Sciences - No. KJCX2-YW-M15 the National Natural Science Foundation of China - No. 91127043, 20911130229 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 |
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| Snippet | The peptide assembly structures of polyglutamine （PolyQ） have been studied by using scanning tunneling microscopy （STM） with high spatial resolution in... The peptide assembly structures of polyglutamine (PolyQ) have been studied by using scanning tunneling microscopy (STM) with high spatial resolution in ambient... |
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| SubjectTerms | adsorption conformation Microscopy odd-even effect peptide Peptides scanning tunneling microscopy 奇偶 导肽 序列 扫描隧道显微镜 显微镜观察 组件结构 组装结构 表面 |
| Title | Odd-Even Sequence Effect of Surface-Mediated Peptide Assemblies Observed by Scanning Tunneling Microscopy |
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