Evidence map›Paper›PMID 33576622›Full record

ArticleACS nano2021

Nanoscale Assembly of Functional Peptides with Divergent Programming Elements.

Ana M Garcia, Michele Melchionna, Ottavia Bellotto, Slavko Kralj, Sabrina Semeraro, Evelina Parisi, Daniel Iglesias, Paola D'Andrea, Rita De Zorzi, Attilio V Vargiu and 1 more

Abstract read
In one paragraph

Article in ACS nano, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Controlling Supramolecular Assembly through Peptide Chirality.ACS applied materials & interfaces · 2025
    Article
  6. Chirality Makes or Breaks Chemically Driven Self-Assembly.Angewandte Chemie (International ed. in English) · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Assessment of the MARTINI 3 Performance for Short Peptide Self-Assembly.Journal of chemical theory and computation · 2024
    Article
  17. Minimal Peptoid Dynamics Inform Self-Assembly Propensity.The journal of physical chemistry. B · 2023
    Article
  18. Review
  19. Article
  20. 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.

Ana M GarciaChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0003-0482-849X
Michele MelchionnaChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0001-9813-9753
Ottavia BellottoChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0003-4434-2865
Slavko KraljChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0002-0771-3818
Sabrina SemeraroChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0002-3707-9117
Evelina ParisiChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.
Daniel IglesiasChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0002-1998-0518
Paola D'AndreaLife Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.
Rita De ZorziChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.
Attilio V VargiuPhysics Department, University of Cagliari, S.P. 8, km. 0.700, 09042 Monserrato, Italy.ORCID 0000-0003-4013-8867
Silvia MarchesanChemical and Pharmaceutical Sciences Department, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0001-6089-3873

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Self-assembling peptides are being applied both in the biomedical area and as building blocks in nanotechnology. Their applications are closely linked to their modes of self-assembly, which determine the functional nanostructures that they form. This work brings together two structural elements that direct nanoscale self-association in divergent directions: proline as a β-breaker and the β-structure-associated diphenylalanine motif, into a single tripeptide sequence. Amino acid chirality was found to resolve the tension inherent to these conflicting self-assembly instructions. Stereoconfiguration determined the ability of each of the eight possible Pro-Phe-Phe stereoisomers to self-associate into diverse nanostructures, including nanoparticles, nanotapes, or fibrils, which yielded hydrogels with gel-to-sol transition at a physiologically relevant temperature. Three single-crystal structures and all-atom molecular dynamics simulations elucidated the ability of each peptide to establish key interactions to form long-range assemblies (

Indexed as

NanostructuresPeptidesAmyloidHydrogelsNanotechnologyAmyloidHydrogelsPeptidesamyloidchiralityd-amino acidshydrogelspeptideprolineself-assembly

Identifiers

PMID33576622
PMCPMC8023796

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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.