Evidence map›Paper›PMID 37543997›Full record

ArticleAmino acids2023

Optimizing the synthesis of dimeric peptides: influence of the reaction medium and effects that modulate kinetics and reaction yield.

Carlos F R C Guimarães, Amanda S Félix, Tiago A S Brandão, Marcelo P Bemquerer, Dorila Piló-Veloso, Rodrigo M Verly, Jarbas M Resende

Abstract read
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In one paragraph

Article in Amino acids, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

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

7 authors at 3 institutions in 1 country.

Carlos F R C GuimarãesDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, P.O. Box 486, Belo Horizonte, MG, 31270-901, Brazil.ORCID http://orcid.org/0000-0002-0610-4201
Amanda S FélixDepartamento de Química, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, MG, 39100-000, Brazil.ORCID http://orcid.org/0000-0003-4074-5966
Tiago A S BrandãoDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, P.O. Box 486, Belo Horizonte, MG, 31270-901, Brazil.ORCID http://orcid.org/0000-0002-7783-3014
Marcelo P BemquererEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA), Embrapa Gado de Leite, Juiz de Fora, MG, 36038-330, Brazil.ORCID http://orcid.org/0000-0002-9740-5818
Dorila Piló-VelosoDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, P.O. Box 486, Belo Horizonte, MG, 31270-901, Brazil.ORCID http://orcid.org/0009-0000-8586-2723
Rodrigo M VerlyDepartamento de Química, Universidade Federal dos Vales do Jequitinhonha e Mucuri, Diamantina, MG, 39100-000, Brazil. verly.rodrigo@ufvjm.edu.br.ORCID http://orcid.org/0000-0003-0356-6862
Jarbas M ResendeDepartamento de Química, Instituto de Ciências Exatas, Universidade Federal de Minas Gerais, P.O. Box 486, Belo Horizonte, MG, 31270-901, Brazil. jmr@ufmg.br.ORCID http://orcid.org/0000-0001-9827-7312
Universidade Federal de Minas Gerais · BRUniversidade Federal dos Vales do Jequitinhonha e Mucuri · BRBrazilian Agricultural Research Corporation · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptides are remarkably interesting alternatives to several applications. In particular, antimicrobial sequences have raised major interest of the scientific community due to the resistance acquired by commonly used antibiotics. Amongst these, some dimeric peptides have shown very promising characteristics as strong biological activities and resistance against degradation by peptidases. However, despite such promising characteristics, a relatively small number of studies address dimeric peptides, mainly due to the synthesis-related obstacles in their production, whereas the well-implemented routines of solid phase peptide synthesis-which includes the possibility of automation-makes life significantly easier. Here, we present kinetic investigations of the dimerization of a cysteine-containing sequence to obtain the homodimeric antimicrobial peptide homotarsinin. Based on the structural and membrane interaction data already available for the dimer and its monomeric chain, we have proposed distinct dimerization protocols in selected environments, namely, aqueous buffer, TFE:H

Indexed as

Antimicrobial PeptidesPeptidesCysteineDimerizationKineticsMicellesProtein MultimerizationAntimicrobial PeptidesCysteineMicellesPeptidesAggregationDimeric peptidesDisulfide bondKineticsPeptide structurePeptide synthesis

Identifiers

PMID37543997
OpenAlexW4385610163

What OpenQuestion holds

Textmetadata
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.