Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation
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Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation. / Song, Yongxiu; Dai, Bin; Wang, Yong; Wang, Yin; Liu, Cong; Gourdon, Pontus; Liu, Lei; Wang, Kaituo; Dong, Mingdong.
I: Nano Letters, Bind 22, Nr. 9, 2022, s. 3707–3712.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation
AU - Song, Yongxiu
AU - Dai, Bin
AU - Wang, Yong
AU - Wang, Yin
AU - Liu, Cong
AU - Gourdon, Pontus
AU - Liu, Lei
AU - Wang, Kaituo
AU - Dong, Mingdong
N1 - Publisher Copyright: ©
PY - 2022
Y1 - 2022
N2 - 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.
AB - 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.
KW - atomic force microscopy
KW - cryo-electron microscopy (cryo-EM)
KW - hierarchical nanostructure
KW - peptide self-assembly
KW - twisted nanofibrils
U2 - 10.1021/acs.nanolett.2c00596
DO - 10.1021/acs.nanolett.2c00596
M3 - Journal article
C2 - 35467349
AN - SCOPUS:85129327725
VL - 22
SP - 3707
EP - 3712
JO - Nano Letters
JF - Nano Letters
SN - 1530-6984
IS - 9
ER -
ID: 311615140