Evidence map›Paper›PMID 33668767›Full record

ReviewMolecules (Basel, Switzerland)2021

Peptide-Protein Interactions: From Drug Design to Supramolecular Biomaterials.

Andrea Caporale, Simone Adorinni, Doriano Lamba, Michele Saviano

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Gold Nanoparticles Guided by Self-Assembling Peptides: From Sequence to Superstructure.Chembiochem : a European journal of chemical biology · 2025
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Unveiling a New Antimicrobial Peptide with Efficacy againstAntibiotics (Basel, Switzerland) · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Self-Assembled Peptide Nanostructures for ECM Biomimicry.Nanomaterials (Basel, Switzerland) · 2022
    Review
  16. New Advances in Short Peptides: Looking Forward.Molecules (Basel, Switzerland) · 2022
    Article
  17. Advances in Research of Short Peptides.Molecules (Basel, Switzerland) · 2022
    Article
  18. Review
  19. 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

4 authors at 3 institutions in 1 country.

Andrea CaporaleIC-CNR, c/o Area Science Park, S.S. 14 Km 163.5 Basovizza, 34149 Trieste, Italy.ORCID 0000-0002-7827-3960
Simone AdorinniDipartimento di Scienze Chimiche e Farmaceutiche di Università di Trieste, Via L. Giorgieri 1, 34127 Trieste, Italy.ORCID 0000-0002-6888-7635
Doriano LambaIC-CNR, c/o Area Science Park, S.S. 14 Km 163.5 Basovizza, 34149 Trieste, Italy.ORCID 0000-0001-6859-7868
Michele SavianoIstituto di Cristallografia, Consiglio Nazionale delle Ricerche (IC-CNR), Via Giovanni Amendola 122/O, 70126 Bari, Italy.
AREA Science Park · ITNational Research Council · ITUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The self-recognition and self-assembly of biomolecules are spontaneous processes that occur in Nature and allow the formation of ordered structures, at the nanoscale or even at the macroscale, under thermodynamic and kinetic equilibrium as a consequence of specific and local interactions. In particular, peptides and peptidomimetics play an elected role, as they may allow a rational approach to elucidate biological mechanisms to develop new drugs, biomaterials, catalysts, or semiconductors. The forces that rule self-recognition and self-assembly processes are weak interactions, such as hydrogen bonding, electrostatic attractions, and van der Waals forces, and they underlie the formation of the secondary structure (e.g., α-helix, β-sheet, polyproline II helix), which plays a key role in all biological processes. Here, we present recent and significant examples whereby design was successfully applied to attain the desired structural motifs toward function. These studies are important to understand the main interactions ruling the biological processes and the onset of many pathologies. The types of secondary structure adopted by peptides during self-assembly have a fundamental importance not only on the type of nano- or macro-structure formed but also on the properties of biomaterials, such as the types of interaction, encapsulation, non-covalent interaction, or covalent interaction, which are ultimately useful for applications in drug delivery.

Indexed as

Drug DesignBiocompatible MaterialsDrug Delivery SystemsMacromolecular SubstancesPeptidesProteinsBiocompatible MaterialsMacromolecular SubstancesPeptidesProteinsamyloidsdrug deliverymolecular recognitionpeptide designpeptide/protein interactions (PPI)peptidomimeticself-assembling peptide (SAP)supramolecular biomaterials

Identifiers

PMID33668767
PMCPMC7956380
OpenAlexW3130319044

What OpenQuestion 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 OpenQuestion graph.