Evidence map›Paper›PMID 37857855›Full record

ArticleCommunications biology2023

Molecular hybridization strategy for tuning bioactive peptide function.

Cibele Nicolaski Pedron, Marcelo Der Torossian Torres, Cyntia Silva Oliveira, Adriana Farias Silva, Gislaine Patricia Andrade, Yiming Wang, Maria Aparecida Silva Pinhal, Giselle Cerchiaro, Pedro Ismael da Silva Junior, Fernanda Dias da Silva and 3 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. 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

13 authors at 6 institutions in 2 countries.

Cibele Nicolaski PedronCentro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, 09210580, Brazil.ORCID http://orcid.org/0000-0002-4188-3589
Marcelo Der Torossian TorresMachine Biology Group, Departments of Psychiatry and Microbiology, Institute for Biomedical Informatics, Institute for Translational Medicine and Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-6165-9138
Cyntia Silva OliveiraDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, 04044020, Brazil.ORCID http://orcid.org/0000-0003-2049-7627
Adriana Farias SilvaDepartamento de Biofísica, Universidade Federal de São Paulo, São Paulo, SP, 04044020, Brazil.
Gislaine Patricia AndradeCentro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, 09210580, Brazil.
Yiming WangDepartments of Bioengineering and Chemical and Biomolecular Engineering, School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0003-3657-6100
Maria Aparecida Silva PinhalDepartamento de Bioquímica, Universidade Federal de São Paulo, São Paulo, SP, 04044020, Brazil.
Giselle CerchiaroCentro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, 09210580, Brazil.
Pedro Ismael da Silva JuniorLaboratório de Toxinologia Aplicada (LETA) - Instituto Butantan, São Paulo, SP, 05503900, Brazil.
Fernanda Dias da SilvaCentro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, 09210580, Brazil.ORCID http://orcid.org/0000-0002-3508-6241
Ravi RadhakrishnanDepartments of Bioengineering and Chemical and Biomolecular Engineering, School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, PA, USA.
Cesar de la Fuente-NunezMachine Biology Group, Departments of Psychiatry and Microbiology, Institute for Biomedical Informatics, Institute for Translational Medicine and Therapeutics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA. cfuente@upenn.edu.ORCID http://orcid.org/0000-0002-2005-5629
Vani Xavier Oliveira JuniorCentro de Ciências Naturais e Humanas, Universidade Federal do ABC, Santo André, SP, 09210580, Brazil. vani.junior@ufabc.edu.br.ORCID http://orcid.org/0000-0002-9420-0956
Universidade Federal do ABC · BRUniversidade Federal de São Paulo · BRUniversity of Pennsylvania · USInstituto Butantan · BRTranslational Therapeutics (United States) · USUniversity City Science Center · US

Funding

TRANSGENIC AND CHIMERIC MOUSE COREP30DK050306 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI GARY D. WU · 1997 to 2026
$32.5M
Regulation of cell, tissue, and nucleus function by mechanical properties of biopolymer networksR35GM136259 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Paul A Janmey · 2020 to 2026
$3.2M
Combining chemical and computational tools for predictive models of microbiome communitiesR35GM138201 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DE LA FUENTE, CESAR · 2020 to 2024
$1.8M
NIDDK NIH HHS P30 DK050306NIGMS NIH HHS R35 GM136259NIGMS NIH HHS R35 GM138201
6 · The paper itself

Abstract

The physicochemical and structural properties of antimicrobial peptides (AMPs) determine their mechanism of action and biological function. However, the development of AMPs as therapeutic drugs has been traditionally limited by their toxicity for human cells. Tuning the physicochemical properties of such molecules may abolish toxicity and yield synthetic molecules displaying optimal safety profiles and enhanced antimicrobial activity. Here, natural peptides were modified to improve their activity by the hybridization of sequences from two different active peptide sequences. Hybrid AMPs (hAMPs) were generated by combining the amphipathic faces of the highly toxic peptide VmCT1, derived from scorpion venom, with parts of four other naturally occurring peptides having high antimicrobial activity and low toxicity against human cells. This strategy led to the design of seven synthetic bioactive variants, all of which preserved their structure and presented increased antimicrobial activity (3.1-128 μmol L

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesAmino Acid SequenceHumansAnti-Infective AgentsAntimicrobial Cationic Peptides

Identifiers

PMID37857855
PMCPMC10587126
OpenAlexW4387773379

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.