Evidence map›Paper›PMID 27447093›Full record

ArticleNanoscale2016

Self-assembly mechanisms of nanofibers from peptide amphiphiles in solution and on substrate surfaces.

Hsien-Shun Liao, Jing Lin, Yang Liu, Peng Huang, Albert Jin, Xiaoyuan Chen

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nanoscale, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 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

6 authors.

Hsien-Shun LiaoDepartment of Mechanical Engineering, National Taiwan University, Taipei 10617, Taiwan and Laboratory of Molecular Imaging and Nanomedicine (LOMIN), National Institute of Biomedical Imaging and Bioengineering (NIBIB), National Institutes of Health, Bethesda, Maryland 20892, USA. shawn.chen@nih.gov and Laboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Biomedical Imaging and Bioengineering (NIBIB), National Institutes of Health, Bethesda, Maryland 20892, USA. jina@mail.nih.gov.
Jing LinGuangdong Key Laboratory for Biomedical Measurements and Ultrasound Imaging, School of Biomedical Engineering, Shenzhen University, Shenzhen 518060, China. peng.huang@szu.edu.cn.
Yang LiuFitzpatrick Institute for Photonics, Department of Biomedical Engineering, Duke University, Durham, NC 27708, USA.
Peng HuangGuangdong Key Laboratory for Biomedical Measurements and Ultrasound Imaging, School of Biomedical Engineering, Shenzhen University, Shenzhen 518060, China. peng.huang@szu.edu.cn.
Albert JinLaboratory of Cellular Imaging and Macromolecular Biophysics, National Institute of Biomedical Imaging and Bioengineering (NIBIB), National Institutes of Health, Bethesda, Maryland 20892, USA. jina@mail.nih.gov.
Xiaoyuan ChenLaboratory of Molecular Imaging and Nanomedicine (LOMIN), National Institute of Biomedical Imaging and Bioengineering (NIBIB), National Institutes of Health, Bethesda, Maryland 20892, USA. shawn.chen@nih.gov.

Funding

Laboratory of Molecular Imaging and NanomedicineZIAEB000073 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI CHEN, XIAOYUAN · 2010 to 2020
$32.8M
Biomedical Studies and Cellular Imaging via Atomic Force MicroscopyZIAEB000015 · NIBIB · NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING · PI JIN, ALBERT J · 2009 to 2025
$5.8M
Intramural NIH HHS Z99 EB999999Intramural NIH HHS ZIA EB000073
6 · The paper itself

Abstract

We report the investigation of the self-assembly mechanism of nanofibers, using a small peptide amphiphile (NapFFKYp) as a model. Combining experimental and simulation methods, we identify the self-assembly pathways in the solution and on the substrates, respectively. In the solution, peptide amphiphiles undergo the nucleation process to grow into nanofibers. The nanofibers can further twist into high-ordered nanofibers with aging. On the substrates, peptide amphiphiles form nanofibers and nanosheet structures simultaneously. This surface-induced nanosheet consists of rod-like structures, and its thickness is substrate-dependent. Most intriguingly, water can transform the nanosheet into the nanofiber. Molecular dynamic simulation suggests that hydrophobic and ion-ion interactions are dominant forces during the self-assembly process.

Indexed as

NanofibersHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationPeptidesWaterPeptidesWater

Identifiers

PMID27447093
PMCPMC5226416

What OpenQuestion holds

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Registered trials

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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.