Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation
(2022) In Nano Letters 22(9). p.3707-3712- Abstract
Amyloid peptide (AP) self-assembly is a hierarchical process. However, the mechanistic rule of guiding peptides to organize well-ordered nanostructure in a clear and precise manner remains poorly understood. Herein we explored the molecular insight of AP motif aggregates underlying hierarchical process with helical fibrillar structure by atomic force microscope, cryo-electron microscopy (cryo-EM), and molecular dynamics simulation. AP assembly encompasses well-ordered twisted fibrils with uniform morphology, size, and periodicity. More importantly, a heterozipper β-sheet was identified in a protofilament of AP assembly determined by cryo-EM with a high resolution of 3.5 Å. Each peptide heterozipper was further composed of two... (More)
Amyloid peptide (AP) self-assembly is a hierarchical process. However, the mechanistic rule of guiding peptides to organize well-ordered nanostructure in a clear and precise manner remains poorly understood. Herein we explored the molecular insight of AP motif aggregates underlying hierarchical process with helical fibrillar structure by atomic force microscope, cryo-electron microscopy (cryo-EM), and molecular dynamics simulation. AP assembly encompasses well-ordered twisted fibrils with uniform morphology, size, and periodicity. More importantly, a heterozipper β-sheet was identified in a protofilament of AP assembly determined by cryo-EM with a high resolution of 3.5 Å. Each peptide heterozipper was further composed of two antiparallel β strands and arranged by an alternative manner in a protofilament. The hydrophobic core and hydrophilic area in each zipper played the significant role for peptide assembling. This work proposed and verified the rule facilitating the basic building unit to form twisted fibrils and gave the explanation of peptide hierarchical assembling.
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- author
- Song, Yongxiu ; Dai, Bin ; Wang, Yong ; Wang, Yin ; Liu, Cong ; Gourdon, Pontus LU ; Liu, Lei ; Wang, Kaituo and Dong, Mingdong
- organization
- publishing date
- 2022
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- atomic force microscopy, cryo-electron microscopy (cryo-EM), hierarchical nanostructure, peptide self-assembly, twisted nanofibrils
- in
- Nano Letters
- volume
- 22
- issue
- 9
- pages
- 3707 - 3712
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:85129327725
- pmid:35467349
- ISSN
- 1530-6984
- DOI
- 10.1021/acs.nanolett.2c00596
- language
- English
- LU publication?
- yes
- id
- 46ff3e6b-e710-477c-b283-f71cc0a358b4
- date added to LUP
- 2022-08-15 12:30:25
- date last changed
- 2024-06-13 18:15:04
@article{46ff3e6b-e710-477c-b283-f71cc0a358b4,
abstract = {{<p>Amyloid peptide (AP) self-assembly is a hierarchical process. However, the mechanistic rule of guiding peptides to organize well-ordered nanostructure in a clear and precise manner remains poorly understood. Herein we explored the molecular insight of AP motif aggregates underlying hierarchical process with helical fibrillar structure by atomic force microscope, cryo-electron microscopy (cryo-EM), and molecular dynamics simulation. AP assembly encompasses well-ordered twisted fibrils with uniform morphology, size, and periodicity. More importantly, a heterozipper β-sheet was identified in a protofilament of AP assembly determined by cryo-EM with a high resolution of 3.5 Å. Each peptide heterozipper was further composed of two antiparallel β strands and arranged by an alternative manner in a protofilament. The hydrophobic core and hydrophilic area in each zipper played the significant role for peptide assembling. This work proposed and verified the rule facilitating the basic building unit to form twisted fibrils and gave the explanation of peptide hierarchical assembling. </p>}},
author = {{Song, Yongxiu and Dai, Bin and Wang, Yong and Wang, Yin and Liu, Cong and Gourdon, Pontus and Liu, Lei and Wang, Kaituo and Dong, Mingdong}},
issn = {{1530-6984}},
keywords = {{atomic force microscopy; cryo-electron microscopy (cryo-EM); hierarchical nanostructure; peptide self-assembly; twisted nanofibrils}},
language = {{eng}},
number = {{9}},
pages = {{3707--3712}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Nano Letters}},
title = {{Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation}},
url = {{http://dx.doi.org/10.1021/acs.nanolett.2c00596}},
doi = {{10.1021/acs.nanolett.2c00596}},
volume = {{22}},
year = {{2022}},
}