Evidence map›Paper›PMID 25268037›Full record

ArticleNano letters2014

Noncanonical self-assembly of highly asymmetric genetically encoded polypeptide amphiphiles into cylindrical micelles.

Jonathan R McDaniel, Isaac Weitzhandler, Sylvain Prevost, Kevin B Vargo, Marie-Sousai Appavou, Daniel A Hammer, Michael Gradzielski, Ashutosh Chilkoti

Open access · greenAbstract read
In one paragraph

Article in Nano letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.4field-weighted citation impact, top 4% of its field
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

31 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
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  11. Preparation of Poly(MTZ)ACS omega · 2020
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  16. Genetically Encoded Cholesterol-Modified Polypeptides.Journal of the American Chemical Society · 2019
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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

8 authors at 5 institutions in 2 countries.

Jonathan R McDanielDepartment of Biomedical Engineering and Research Triangle MRSEC, Duke University , Durham, North Carolina 27708, United States.
Isaac Weitzhandler
Sylvain Prevost
Kevin B Vargo
Marie-Sousai Appavou
Daniel A Hammer
Michael Gradzielski
Ashutosh Chilkoti
Duke University · USTechnische Universität Berlin · DEUniversity of Pennsylvania · USForschungszentrum Jülich · DEResearch Triangle Park Foundation · US

Funding

ELASTIN FUSION PROTEINSR01GM061232 · NIGMS · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2000 to 2017
$4.6M
NIGMS NIH HHS R01 GM061232NIGMS NIH HHS R01 GM-61232
6 · The paper itself

Abstract

Elastin-like polypeptides (ELPs) are a class of biopolymers consisting of the pentameric repeat (VPGαG)n based on the sequence of mammalian tropoelastin that display a thermally induced soluble-to-insoluble phase transition in aqueous solution. We have discovered a remarkably simple approach to driving the spontaneous self-assembly of high molecular weight ELPs into nanostructures by genetically fusing a short 1.5 kDa (XGy)z assembly domain to one end of the ELP. Classical theories of self-assembly based on the geometric mass balance of hydrophilic and hydrophobic block copolymers suggest that these highly asymmetric polypeptides should form spherical micelles. Surprisingly, when sufficiently hydrophobic amino acids (X) are presented in a periodic sequence such as (FGG)8 or (YG)8, these highly asymmetric polypeptides self-assemble into cylindrical micelles whose length can be tuned by the sequence of the morphogenic tag. These nanostructures were characterized by light scattering, tunable resistive pulse sensing, fluorescence spectrophotometry, and thermal turbidimetry, as well as by cryogenic transmission electron microscopy (cryo-TEM) and small-angle neutron scattering (SANS). These short assembly domains provide a facile strategy to control the size, shape, and stability of stimuli responsive polypeptide nanostructures.

Indexed as

MicellesAmino Acid SequenceBiocompatible MaterialsElastinHydrophobic and Hydrophilic InteractionsMolecular Sequence DataNanostructuresParticle SizePeptidesPhase TransitionRecombinant ProteinsBiocompatible MaterialsElastinMicellesPeptidesRecombinant Proteinsbiomaterialscryo-TEMelastin-like polypeptidesprotein polymersSelf-assemblysmall-angle neutron scattering

Identifiers

PMID25268037
PMCPMC4246002
OpenAlexW2332588081

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.