Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide
The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity....
| Main Authors: | , , , , , , , , |
|---|---|
| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2017
|
| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/85006 http://hdl.handle.net/10220/42054 |
| _version_ | 1826122324763475968 |
|---|---|
| author | Liu, Lei Li, Qiang Zhang, Shuai Wang, Xiaofeng Hoffmann, Søren Vrønning Li, Jingyuan Liu, Zheng Besenbacher, Flemming Dong, Mingdong |
| author2 | School of Materials Science & Engineering |
| author_facet | School of Materials Science & Engineering Liu, Lei Li, Qiang Zhang, Shuai Wang, Xiaofeng Hoffmann, Søren Vrønning Li, Jingyuan Liu, Zheng Besenbacher, Flemming Dong, Mingdong |
| author_sort | Liu, Lei |
| collection | NTU |
| description | The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ33-42 aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ33-42 consisting of novel parallel β-strand-like structure is further revealed by means of a quantitative nanomechanical spectroscopy technique with force controlled in pico-Newton range, combining with molecular dynamic simulation. The identified parallel β-strand-like structure of molecular monolayer is distinct from the antiparallel β-strand structure of Aβ33-42 amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease. |
| first_indexed | 2024-10-01T05:46:38Z |
| format | Journal Article |
| id | ntu-10356/85006 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T05:46:38Z |
| publishDate | 2017 |
| record_format | dspace |
| spelling | ntu-10356/850062023-07-14T15:46:46Z Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide Liu, Lei Li, Qiang Zhang, Shuai Wang, Xiaofeng Hoffmann, Søren Vrønning Li, Jingyuan Liu, Zheng Besenbacher, Flemming Dong, Mingdong School of Materials Science & Engineering Atomic force microscopy Amyloid peptide aggregation The differentiation of protein properties and biological functions arises from the variation in the primary and secondary structure. Specifically, in abnormal assemblies of protein, such as amyloid peptide, the secondary structure is closely correlated with the stable ensemble and the cytotoxicity. In this work, the early Aβ33-42 aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide Aβ33-42 consisting of novel parallel β-strand-like structure is further revealed by means of a quantitative nanomechanical spectroscopy technique with force controlled in pico-Newton range, combining with molecular dynamic simulation. The identified parallel β-strand-like structure of molecular monolayer is distinct from the antiparallel β-strand structure of Aβ33-42 amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease. Published version 2017-01-19T06:26:22Z 2019-12-06T15:55:22Z 2017-01-19T06:26:22Z 2019-12-06T15:55:22Z 2016 Journal Article Liu, L., Li, Q., Zhang, S., Wang, X., Hoffmann, S. V., Li, J., et al. (2016). Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide. Advanced Science, 3(6), 1500369-. https://hdl.handle.net/10356/85006 http://hdl.handle.net/10220/42054 10.1002/advs.201500369 27818898 en Advanced Science © 2016 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. 10 p. application/pdf |
| spellingShingle | Atomic force microscopy Amyloid peptide aggregation Liu, Lei Li, Qiang Zhang, Shuai Wang, Xiaofeng Hoffmann, Søren Vrønning Li, Jingyuan Liu, Zheng Besenbacher, Flemming Dong, Mingdong Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title | Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title_full | Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title_fullStr | Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title_full_unstemmed | Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title_short | Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide |
| title_sort | identification of a novel parallel β strand conformation within molecular monolayer of amyloid peptide |
| topic | Atomic force microscopy Amyloid peptide aggregation |
| url | https://hdl.handle.net/10356/85006 http://hdl.handle.net/10220/42054 |
| work_keys_str_mv | AT liulei identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT liqiang identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT zhangshuai identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT wangxiaofeng identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT hoffmannsørenvrønning identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT lijingyuan identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT liuzheng identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT besenbacherflemming identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide AT dongmingdong identificationofanovelparallelbstrandconformationwithinmolecularmonolayerofamyloidpeptide |