Evidence map›Paper›PMID 33922150›Full record

ArticleMembranes2021

Modulatory Effects of Acidic pH and Membrane Potential on the Adsorption of pH-Sensitive Peptides to Anionic Lipid Membrane.

Dayane Dos Santos Alvares, Ingrid Bernardes Santana Martins, Taisa Giordano Viegas, Mario Sergio Palma, Alexandre Suman de Araujo, Sidney Jurado de Carvalho, João Ruggiero Neto

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 14 citations in OpenAlex.

  1. Improving the Estimation of pThe journal of physical chemistry. B · 2026
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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

7 authors at 1 institution in 1 country.

Dayane Dos Santos AlvaresIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0002-6521-9148
Ingrid Bernardes Santana MartinsIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0001-9970-6035
Taisa Giordano ViegasIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0002-8315-1300
Mario Sergio PalmaInstitute of Biosciences, Department of Basic and Applied Biology, UNESP-São Paulo State University, Rio Claro 13506-752, SP, Brazil.ORCID 0000-0002-7363-8211
Alexandre Suman de AraujoIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0001-9376-9748
Sidney Jurado de CarvalhoIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0002-9763-2797
João Ruggiero NetoIBILCE, Department of Physics, UNESP-São Paulo State University, São José do Rio Preto 15054-000, SP, Brazil.ORCID 0000-0002-2283-3316
Universidade Estadual Paulista (Unesp) · BR

Funding

São Paulo Research Foundation-FAPESP 2010/18169-3São Paulo Research Foundation-FAPESP 2015/25619-9São Paulo Research Foundation-FAPESP 2015/25620-7São Paulo Research Foundation-FAPESP 2016/16212-5São Paulo Research Foundation-FAPESP 2018/01841-2
6 · The paper itself

Abstract

Anionic lipid membrane electrostatic potential and solution pH can influence cationic peptide adsorption to these bilayers, especially those containing simultaneously acid and basic residues. Here, we investigate the effects of the pH solution on MP1 (IDWKKLLDAAKQIL-NH2) adsorption to anionic (7POPC:3POPG) lipid vesicles in comparison to its analog H-MP1, with histidines substituting lysines. We used the association of adsorption isotherms and constant pH molecular dynamic simulations (CpHMD) to explore the effects of membrane potential and pH on peptides' adsorption on this lipid membrane. We analyzed the fluorescence and zeta potential adsorption isotherms using the Gouy-Chapman theory. In CpHMD simulations for the peptides in solution and adsorbed on the lipid bilayer, we used the conformations obtained by conventional MD simulations at a μs timescale. Non-equilibrium Monte Carlo simulations provided the protonation states of acidic and basic residues. CpHMD showed average pKa shifts of two to three units, resulting in a higher net charge for the analog than for MP1, strongly modulating the peptide adsorption. The fractions of the protonation of acidic and basic residues and the peptides' net charges obtained from the analysis of the adsorption isotherms were in reasonable agreement with those from CpHMD. MP1 adsorption was almost insensitive to solution pH. H-MP1 was much more sensitive to partitioning, at acidic pH, with an affinity ten times higher than in neutral ones.

Indexed as

CpHMDfluorescence spectroscopymembrane potentialpH-responsive peptideszeta potential

Identifiers

PMID33922150
PMCPMC8143466
OpenAlexW3156657419

What OpenQuestion holds

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LicenceCC BY
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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.