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Søren Vrønning Hoffmann

Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide

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Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide. / Liu, Lei; Li, Qiang; Zhang, Shuai; Wang, Xiaofeng; Hoffmann, Soren Vronning; Li, Jingyuan; Liu, Zheng; Besenbacher, Flemming; Dong, Mingdong.

I: Advanced Science, Bind 3, Nr. 6, 1500369, 06.2016.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Liu, Lei ; Li, Qiang ; Zhang, Shuai ; Wang, Xiaofeng ; Hoffmann, Soren Vronning ; Li, Jingyuan ; Liu, Zheng ; Besenbacher, Flemming ; Dong, Mingdong. / Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide. I: Advanced Science. 2016 ; Bind 3, Nr. 6.

Bibtex

@article{9002ab830b764f128300261495d18c6e,
title = "Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide",
abstract = "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 A beta(33-42) aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide A beta(33-42) consisting of novel parallel beta-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 beta-strand-like structure of molecular monolayer is distinct from the antiparallel beta-strand structure of A beta(33-42) amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.",
keywords = "ALZHEIMERS-DISEASE, FORCE MICROSCOPY, FIBRIL FORMATION, PROTEIN, OLIGOMERS, SPECTROSCOPY, MECHANISM, BEAMLINES, TOXICITY, MODEL",
author = "Lei Liu and Qiang Li and Shuai Zhang and Xiaofeng Wang and Hoffmann, {Soren Vronning} and Jingyuan Li and Zheng Liu and Flemming Besenbacher and Mingdong Dong",
year = "2016",
month = jun,
doi = "10.1002/advs.201500369",
language = "English",
volume = "3",
journal = "Advanced Science",
issn = "2198-3844",
publisher = "Wiley",
number = "6",

}

RIS

TY - JOUR

T1 - Identification of a Novel Parallel beta-Strand Conformation within Molecular Monolayer of Amyloid Peptide

AU - Liu, Lei

AU - Li, Qiang

AU - Zhang, Shuai

AU - Wang, Xiaofeng

AU - Hoffmann, Soren Vronning

AU - Li, Jingyuan

AU - Liu, Zheng

AU - Besenbacher, Flemming

AU - Dong, Mingdong

PY - 2016/6

Y1 - 2016/6

N2 - 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 A beta(33-42) aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide A beta(33-42) consisting of novel parallel beta-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 beta-strand-like structure of molecular monolayer is distinct from the antiparallel beta-strand structure of A beta(33-42) amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.

AB - 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 A beta(33-42) aggregates forming the molecular monolayer at hydrophobic interface are investigated. The molecular monolayer of amyloid peptide A beta(33-42) consisting of novel parallel beta-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 beta-strand-like structure of molecular monolayer is distinct from the antiparallel beta-strand structure of A beta(33-42) amyloid fibril. This finding enriches the molecular structures of amyloid peptide aggregation, which could be closely related to the pathogenesis of amyloid disease.

KW - ALZHEIMERS-DISEASE

KW - FORCE MICROSCOPY

KW - FIBRIL FORMATION

KW - PROTEIN

KW - OLIGOMERS

KW - SPECTROSCOPY

KW - MECHANISM

KW - BEAMLINES

KW - TOXICITY

KW - MODEL

U2 - 10.1002/advs.201500369

DO - 10.1002/advs.201500369

M3 - Journal article

C2 - 27818898

VL - 3

JO - Advanced Science

JF - Advanced Science

SN - 2198-3844

IS - 6

M1 - 1500369

ER -