Evidence map›Paper›PMID 33590708›Full record

ReviewSmall (Weinheim an der Bergstrasse, Germany)2021

De Novo Designed Peptide and Protein Hairpins Self-Assemble into Sheets and Nanoparticles.

Johanna M Galloway, Harriet E V Bray, Deborah K Shoemark, Lorna R Hodgson, Jennifer Coombs, Judith M Mantell, Ruth S Rose, James F Ross, Caroline Morris, Robert L Harniman and 4 more

Abstract readReview
In one paragraph

Review in Small (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
  5. Review
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  7. Review
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

14 authors.

Johanna M GallowaySchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.ORCID 0000-0003-3998-0870
Harriet E V BraySchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Deborah K ShoemarkSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Lorna R HodgsonSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Jennifer CoombsSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Judith M MantellSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Ruth S RoseSchool of Biological and Chemical Sciences, Fogg Building, Queen Mary University of London, Mile End Road, London, E1 4QD, UK.
James F RossSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Caroline MorrisSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Robert L HarnimanSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Christopher W WoodSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Christopher ArthurSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.
Paul VerkadeSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol, BS8 1TD, UK.
Derek N WoolfsonSchool of Chemistry, University of Bristol, Cantock's Close, Bristol, BS8 1TS, UK.

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/L014181/1
6 · The paper itself

Abstract

The design and assembly of peptide-based materials has advanced considerably, leading to a variety of fibrous, sheet, and nanoparticle structures. A remaining challenge is to account for and control different possible supramolecular outcomes accessible to the same or similar peptide building blocks. Here a de novo peptide system is presented that forms nanoparticles or sheets depending on the strategic placement of a "disulfide pin" between two elements of secondary structure that drive self-assembly. Specifically, homodimerizing and homotrimerizing de novo coiled-coil α-helices are joined with a flexible linker to generate a series of linear peptides. The helices are pinned back-to-back, constraining them as hairpins by a disulfide bond placed either proximal or distal to the linker. Computational modeling indicates, and advanced microscopy shows, that the proximally pinned hairpins self-assemble into nanoparticles, whereas the distally pinned constructs form sheets. These peptides can be made synthetically or recombinantly to allow both chemical modifications and the introduction of whole protein cargoes as required.

Indexed as

NanoparticlesPeptidesBiophysical PhenomenaProteinsProtein Structure, SecondaryPeptidesProteinscoiled coilcomputational modelingpeptide designprotein designself-assembly

Identifiers

PMID33590708
PMCPMC11475375

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.