Evidence map›Paper›PMID 31783657›Full record

ArticleAntibiotics (Basel, Switzerland)2019

Increases in Hydrophilicity and Charge on the Polar Face of Alyteserin 1c Helix Change its Selectivity towards Gram-Positive Bacteria.

Yamil Liscano, Constain H Salamanca, Lina Vargas, Stefania Cantor, Valentina Laverde-Rojas, José Oñate-Garzón

Open access · goldAbstract read
In one paragraph

Article in Antibiotics (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.5field-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

23 citing papers in PubMed, 52 citations in OpenAlex.

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  7. Understanding the selectivityFrontiers in bioinformatics · 2025
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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

6 authors at 3 institutions in 1 country.

Yamil LiscanoGrupo de Génetica, Regeneración y Cáncer, Instituto de Química, Facultad de Ciencias Exactas y Naturales, Universidad de Antioquia, A.A., Medellín 1226, Colombia.
Constain H SalamancaLaboratorio de Diseño y Formulación de Productos Químicos y Derivados, Departamento de Ciencias Farmacéuticas, Facultad de Ciencias Naturales, Universidad Icesi, Cali 760035, Colombia.
Lina VargasGrupo de Investigación en Química y Biotecnología (QUIBIO), Facultad de Ciencias Básicas, Universidad Santiago de Cali, Calle 5 No. 62-00, Cali 760035, Colombia.
Stefania CantorGrupo de Investigación en Química y Biotecnología (QUIBIO), Facultad de Ciencias Básicas, Universidad Santiago de Cali, Calle 5 No. 62-00, Cali 760035, Colombia.
Valentina Laverde-RojasGrupo de Investigación en Química y Biotecnología (QUIBIO), Facultad de Ciencias Básicas, Universidad Santiago de Cali, Calle 5 No. 62-00, Cali 760035, Colombia.
José Oñate-GarzónGrupo de Investigación en Química y Biotecnología (QUIBIO), Facultad de Ciencias Básicas, Universidad Santiago de Cali, Calle 5 No. 62-00, Cali 760035, Colombia.
Universidad Santiago de Cali · COIcesi University · COUniversidad de Antioquia · CO

Funding

undefined <span style="color:gray;font-size:10px;">undefined</span> 512-621116-A30
6 · The paper itself

Abstract

Recently, resistance of pathogens towards conventional antibiotics has increased, representing a threat to public health globally. As part of the fight against this, studies on alternative antibiotics such as antimicrobial peptides have been performed, and it has been shown that their sequence and structure are closely related to their antimicrobial activity. Against this background, we here evaluated the antibacterial activity of two peptides developed by solid-phase synthesis, Alyteserin 1c (WT) and its mutant derivative (ΔM), which shows increased net charge and reduced hydrophobicity. These structural characteristics were modified as a result of amino acid substitutions on the polar face of the WT helix. The minimum inhibitory concentration (MIC) of both peptides was obtained in Gram-positive and Gram-negative bacteria. The results showed that the rational substitutions of the amino acids increased the activity in Gram-positive bacteria, especially against

Indexed as

Antimicrobial peptideantimicrobial selectivitymembrane modelnet chargeα-helix

Identifiers

PMID31783657
PMCPMC6963856
OpenAlexW2990625890

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.