Evidence map›Paper›PMID 27387853›Full record

ArticleThe journal of physical chemistry letters2016

Structural and Mechanical Properties of Amyloid Beta Fibrils: A Combined Experimental and Theoretical Approach.

Thomas J Paul, Zachary Hoffmann, Congzhou Wang, Maruda Shanmugasundaram, Jason DeJoannis, Alexander Shekhtman, Igor K Lednev, Vamsi K Yadavalli, Rajeev Prabhakar

Abstract read
In one paragraph

Article in The journal of physical chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Thomas J PaulDepartment of Chemistry, University of Miami , Coral Gables, Florida 33146, United States.
Zachary HoffmannDepartment of Chemistry, University of Miami , Coral Gables, Florida 33146, United States.
Congzhou WangDepartment of Chemical and Life Science Engineering, Virginia Commonwealth University , Richmond, Virginia 23284, United States.
Maruda ShanmugasundaramDepartment of Chemistry, University at Albany, State University of New York , Albany, New York 12222, United States.
Jason DeJoannisDassault Systèmes BIOVIA , San Deigo, California 92121, United States.
Alexander ShekhtmanDepartment of Chemistry, University at Albany, State University of New York , Albany, New York 12222, United States.
Igor K LednevDepartment of Chemistry, University at Albany, State University of New York , Albany, New York 12222, United States.
Vamsi K YadavalliDepartment of Chemical and Life Science Engineering, Virginia Commonwealth University , Richmond, Virginia 23284, United States.
Rajeev PrabhakarDepartment of Chemistry, University of Miami , Coral Gables, Florida 33146, United States.

Funding

Real Time (RT) In-cell NMR technology to study protein interactions in live cellsR01GM085006 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHEKHTMAN, ALEXANDER · 2010 to 2021
$2.4M
NIGMS NIH HHS R01 GM085006
6 · The paper itself

Abstract

In this combined experimental (deep ultraviolet resonance Raman (DUVRR) spectroscopy and atomic force microscopy (AFM)) and theoretical (molecular dynamics (MD) simulations and stress-strain (SS)) study, the structural and mechanical properties of amyloid beta (Aβ40) fibrils have been investigated. The DUVRR spectroscopy and AFM experiments confirmed the formation of linear, unbranched and β-sheet rich fibrils. The fibrils (Aβ40)n, formed using n monomers, were equilibrated using all-atom MD simulations. The structural properties such as β-sheet character, twist, interstrand distance, and periodicity of these fibrils were found to be in agreement with experimental measurements. Furthermore, Young's modulus (Y) = 4.2 GPa computed using SS calculations was supported by measured values of 1.79 ± 0.41 and 3.2 ± 0.8 GPa provided by two separate AFM experiments. These results revealed size dependence of structural and material properties of amyloid fibrils and show the utility of such combined experimental and theoretical studies in the design of precisely engineered biomaterials.

Identifiers

PMID27387853
PMCPMC5956519

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.