Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Nano Letters, Vol. 22, No. 9, 2022, p. 3707–3712.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Song, Y, Dai, B, Wang, Y, Wang, Y, Liu, C, Gourdon, P, Liu, L, Wang, K & Dong, M 2022, 'Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation', Nano Letters, vol. 22, no. 9, pp. 3707–3712. https://doi.org/10.1021/acs.nanolett.2c00596

APA

Song, Y., Dai, B., Wang, Y., Wang, Y., Liu, C., Gourdon, P., Liu, L., Wang, K., & Dong, M. (2022). Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation. Nano Letters, 22(9), 3707–3712. https://doi.org/10.1021/acs.nanolett.2c00596

Vancouver

Song Y, Dai B, Wang Y, Wang Y, Liu C, Gourdon P et al. Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation. Nano Letters. 2022;22(9):3707–3712. https://doi.org/10.1021/acs.nanolett.2c00596

Author

Song, Yongxiu ; Dai, Bin ; Wang, Yong ; Wang, Yin ; Liu, Cong ; Gourdon, Pontus ; Liu, Lei ; Wang, Kaituo ; Dong, Mingdong. / Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation. In: Nano Letters. 2022 ; Vol. 22, No. 9. pp. 3707–3712.

Bibtex

@article{8e0dc3296a9f48efa6f398e2be4c2f01,

title = "Identifying Heterozipper β-Sheet in Twisted Amyloid Aggregation",

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 {\AA}. 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. ",

keywords = "atomic force microscopy, cryo-electron microscopy (cryo-EM), hierarchical nanostructure, peptide self-assembly, twisted nanofibrils",

author = "Yongxiu Song and Bin Dai and Yong Wang and Yin Wang and Cong Liu and Pontus Gourdon and Lei Liu and Kaituo Wang and Mingdong Dong",

note = "Publisher Copyright: {\textcopyright} ",

year = "2022",

doi = "10.1021/acs.nanolett.2c00596",

language = "English",

volume = "22",

pages = "3707–3712",

journal = "Nano Letters",

issn = "1530-6984",

publisher = "American Chemical Society",

number = "9",

}

RIS

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