Evidence map›Paper›PMID 35037351›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Mapping the Morphological Landscape of Oligomeric Di-block Peptide-Polymer Amphiphiles.

Benjamin P Allen, Zoe M Wright, Hailey F Taylor, Thomas J Oweida, Sabila Kader-Pinky, Emily F Patteson, Kara M Bucci, Caleb A Cox, Abishec Sundar Senthilvel, Yaroslava G Yingling and 1 more

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

11 authors.

Benjamin P AllenDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.ORCID 0000-0002-2742-9099
Zoe M WrightDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.ORCID 0000-0003-2090-1538
Hailey F TaylorDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Thomas J OweidaDepartment of Material Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Sabila Kader-PinkyDepartment of Material Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Emily F PattesonDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Kara M BucciDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Caleb A CoxDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Abishec Sundar SenthilvelDepartment of Material Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Yaroslava G YinglingDepartment of Material Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.ORCID 0000-0002-8557-9992
Abigail S KnightDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.ORCID 0000-0003-1524-473X

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
NCI NIH HHS P30 CA016086NIGMS NIH HHS T32 GM008570
6 · The paper itself

Abstract

Peptide-polymer amphiphiles (PPAs) are tunable hybrid materials that achieve complex assembly landscapes by combining the sequence-dependent properties of peptides with the structural diversity of polymers. Despite their promise as biomimetic materials, determining how polymer and peptide properties simultaneously affect PPA self-assembly remains challenging. We herein present a systematic study of PPA structure-assembly relationships. PPAs containing oligo(ethyl acrylate) and random-coil peptides were used to determine the role of oligomer molecular weight, dispersity, peptide length, and charge density on self-assembly. We observed that PPAs predominantly formed spheres rather than anisotropic particles. Oligomer molecular weight and peptide hydrophilicity dictated morphology, while dispersity and peptide charge affected particle size. These key benchmarks will facilitate the rational design of PPAs that expand the scope of biomimetic functionality within assembled soft materials.

Indexed as

PeptidesPolymersBiomimeticsHydrophobic and Hydrophilic InteractionsParticle SizePeptidesPolymersBiomimeticElectron MicroscopyPeptide-Polymer AmphiphileSelf-AssemblySupramolecular Chemistry

Identifiers

PMID35037351
PMCPMC8957712

What OpenQuestion holds

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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.