Evidence map›Paper›PMID 36310605›Full record

ArticleFrontiers in molecular biosciences2022

PEGylation of the antimicrobial peptide LyeTx I-b maintains structure-related biological properties and improves selectivity.

Júlio César Moreira Brito, Lucas Raposo Carvalho, Amanda Neves de Souza, Guilherme Carneiro, Paula Prazeres Magalhães, Luiz Macêdo Farias, Natália Rocha Guimarães, Rodrigo Moreira Verly, Jarbas Magalhães Resende, Maria Elena de Lima

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
–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

17 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. The Synthetic Peptide LyeTx I mn∆K, Derived fromAntibiotics (Basel, Switzerland) · 2024
    Article
  13. Drug Discovery and the Supramolecular Factor.ACS medicinal chemistry letters · 2023
    Article
  14. Review
  15. Article
  16. Review
  17. 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

10 authors.

Júlio César Moreira BritoFundação Ezequiel Dias, Diretoria de Pesquisa e Desenvolvimento, Belo Horizonte, MG, Brazil.
Lucas Raposo CarvalhoDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
Amanda Neves de SouzaDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, MG, Brazil.
Guilherme CarneiroDepartamento de Farmácia, Faculdade de Ciências Biológicas e da Saúde, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, MG, Brazil.
Paula Prazeres MagalhãesDepartamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
Luiz Macêdo FariasDepartamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
Natália Rocha GuimarãesDepartamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
Rodrigo Moreira VerlyDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, MG, Brazil.
Jarbas Magalhães ResendeDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
Maria Elena de LimaPrograma de Pós-graduação em Medicina e Biomedicina da Santa Casa de Belo Horizonte, Belo Horizonte, MG, Brazil.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The biological activity of antimicrobial peptides and proteins is closely related to their structural aspects and is sensitive to certain post-translational modifications such as glycosylation, lipidation and PEGylation. However, PEGylation of protein and peptide drugs has expanded in recent years due to the reduction of their toxicity. Due to their size, the PEGylation process can either preserve or compromise the overall structure of these biopolymers and their biological properties. The antimicrobial peptide LyeTx I-b

Indexed as

antimicrobial peptideLyeTx I-bPEGylationpeptide-membrane interactionpost-translational modificationstructure

Identifiers

PMID36310605
PMCPMC9611540

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.