Evidence map›Paper›PMID 37358231›Full record

ArticleACS nano2023

Stability of Nanopeptides: Structure and Molecular Exchange of Self-assembled Peptide Fibers.

Nico König, Szymon Mikolaj Szostak, Josefine Eilsø Nielsen, Martha Dunbar, Su Yang, Weike Chen, Ari Benjamin, Aurel Radulescu, Najet Mahmoudi, Lutz Willner and 3 more

Open access · hybridAbstract read
In one paragraph

Article in ACS nano, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

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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

13 authors at 5 institutions in 4 countries.

Nico KönigDepartment of Chemistry, University of Oslo, P.O. Box 1033 Blindern, 0315 Oslo, Norway.ORCID 0000-0003-3319-5708
Szymon Mikolaj SzostakDepartment of Chemistry, University of Oslo, P.O. Box 1033 Blindern, 0315 Oslo, Norway.ORCID 0000-0002-3057-6225
Josefine Eilsø NielsenDepartment of Chemistry, University of Oslo, P.O. Box 1033 Blindern, 0315 Oslo, Norway.ORCID 0000-0001-9274-5533
Martha DunbarDepartment of Mechanical Engineering, Northwestern University, Evanston, Illinois 60208, United States.ORCID 0000-0002-2289-6982
Su YangDepartment of Chemistry & Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019, United States.
Weike ChenDepartment of Chemistry & Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019, United States.
Ari BenjaminDepartment of Mechanical Engineering, Northwestern University, Evanston, Illinois 60208, United States.
Aurel RadulescuJülich Centre for Neutron Science (JCNS) at Heinz Maier-Leibnitz Zentrum (MLZ), Forschungszentrum Jülich GmbH, 85747 Garching, Germany.
Najet MahmoudiISIS-STFC, Rutherford Appleton Laboratory, Chilton, Oxon OX11 0QX, United Kingdom.
Lutz WillnerJülich Centre for Neutron Science (JCNS-1) and Institute for Biological Information Processing (IBI-8), Forschungszentrum Jülich GmbH, 52425 Jülich, Germany.
Sinan KetenDepartment of Mechanical Engineering, Northwestern University, Evanston, Illinois 60208, United States.ORCID 0000-0003-2203-1425
He DongDepartment of Chemistry & Biochemistry, The University of Texas at Arlington, Arlington, Texas 76019, United States.ORCID 0000-0002-8494-0475
Reidar LundDepartment of Chemistry, University of Oslo, P.O. Box 1033 Blindern, 0315 Oslo, Norway.ORCID 0000-0001-8017-6396
Forschungszentrum Jülich · DENorthwestern University · USThe University of Texas at Arlington · USUniversity of Oslo · NORutherford Appleton Laboratory · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Often nanostructures formed by self-assembly of small molecules based on hydrophobic interactions are rather unstable, causing morphological changes or even dissolution when exposed to changes in aqueous media. In contrast, peptides offer precise control of the nanostructure through a range of molecular interactions where physical stability can be engineered in and, to a certain extent, decoupled from size via rational design. Here, we investigate a family of peptides that form beta-sheet nanofibers and demonstrate a remarkable physical stability even after attachment of poly(ethylene glycol). We employed small-angle neutron/X-ray scattering, circular dichroism spectroscopy, and molecular dynamics simulation techniques to investigate the detailed nanostructure, stability, and molecular exchange. The results for the most stable sequence did not reveal any structural alterations or unimer exchange for temperatures up to 85 °C in the biologically relevant pH range. Only under severe mechanical perturbation (i.e., tip sonication) would the fibers break up, which is reflected in a very high activation barrier for unimer exchange of ∼320 kJ/mol extracted from simulations. The results give important insight into the relation between molecular structure and stability of peptide nanostructure that is important for, e.g., biomedical applications.

Indexed as

NanofibersNanostructuresMolecular Dynamics SimulationPeptidesProtein Conformation, beta-StrandPeptidescomputer simulationmolecular exchangenanostructured peptidesPeptide-assemblypeptide−polymer conjugatessmall-angle scatteringstructural stability

Identifiers

PMID37358231
PMCPMC10339792
OpenAlexW4382011422

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.