Evidence map›Paper›PMID 38526724›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Understanding the Structural Requirements of Peptide-Protein Interaction and Applications for Peptidomimetic Development.

Angy Liseth Davalos Macias, Lilian Costa Alecrim, Fabio C L Almeida, Ricardo Jose Giordano

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Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Angy Liseth Davalos MaciasBiochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil.
Lilian Costa AlecrimBiochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil.
Fabio C L AlmeidaInstitute of Medical Biochemistry, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
Ricardo Jose GiordanoBiochemistry Department, Institute of Chemistry, University of Sao Paulo, Sao Paulo, Brazil. giordano@iq.usp.br.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein-protein interaction is at the heart of most biological processes, and small peptides that bind to protein binding sites are resourceful tools to explore and understand the structural requirements for these interactions. In that sense, phage display is a well-suited technology to study protein-protein interactions, as it allows for unbiased screening of billions of peptides in search for those that interact with a protein binding domain. Here, we will illustrate how two distinct but complementary approaches, phage display and nuclear magnetic resonance (NMR), can be utilized to unveil structural details of peptide-protein interaction. Finally, knowledge derived from phage mutagenesis and NMR studies can be streamlined for quick peptidomimetic design and synthesis using the retroinversion approach to validate using in vitro and in vivo assays the therapeutic potential of peptides identified by phage display.

Indexed as

PeptidomimeticsCell Surface Display TechniquesPeptide LibraryPeptidesProteinsPeptide LibraryPeptidesPeptidomimeticsProteinsNMRNuclear magnetic resonance (NMR)Nuclear magnetic resonancePeptide and protein interactionPeptidomimetic designPhage displayPhage mutagenesis

Identifiers

PMID38526724

What OpenQuestion holds

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Registered trials

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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.