Evidence map›Paper›PMID 36557189›Full record

ArticleMembranes2022

A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models.

Cristiano Giordani, Stefano Russo, Cristina Torrisi, Silvia Morante, Francesco Castelli, Maria Grazia Sarpietro

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2022. 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
0.1field-weighted citation impact, top 55% 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

6 authors at 3 institutions in 2 countries.

Cristiano GiordaniGrupo Productos Naturales Marinos, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia, Calle 70 No. 52-21, Medellín 050010, Colombia.
Stefano RussoDipartimento di Scienze del Farmaco e della Salute, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0001-7539-0427
Cristina TorrisiDipartimento di Scienze del Farmaco e della Salute, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Silvia MoranteDipartimento di Fisica, University of Rome Tor Vergata and Istituto Nazionale di Fisica Nucleare (INFN), Via della Ricerca Scientifica 1, 00133 Roma, Italy.
Francesco CastelliDipartimento di Scienze del Farmaco e della Salute, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.
Maria Grazia SarpietroDipartimento di Scienze del Farmaco e della Salute, Università degli Studi di Catania, Viale A. Doria 6, 95125 Catania, Italy.ORCID 0000-0002-6799-4754
University of Catania · ITUniversidad de Antioquia · COUniversity of Rome Tor Vergata · IT

Funding

University of Antioquia 2020-39532
6 · The paper itself

Abstract

Investigation of the interaction between drugs and biomembrane models, as a strategy to study and eventually improve drug/substrate interactions, is a crucial factor in preliminary screening. Synthesized peptides represent a source of potential anticancer and theragnostic drugs. In this study, we investigated the interaction of a novel synthesized peptide, called RH-23, with a simplified dimyristoylphosphatidylcholine (DMPC) model of the cellular membrane. The interaction of RH-23 with DMPC, organized either in multilamellar vesicles (MLVs) and in Langmuir-Blodgett (LB) monolayers, was assessed using thermodynamic techniques, namely differential scanning calorimetry (DSC) and LB. The calorimetric evaluations showed that RH-23 inserted into MLVs, causing a stabilization of the phospholipid gel phase that increased with the molar fraction of RH-23. Interplay with LB monolayers revealed that RH-23 interacted with DMPC molecules. This work represents the first experimental thermodynamic study on the interaction between RH-23 and a simplified model of the lipid membrane, thus providing a basis for further evaluations of the effect of RH-23 on biological membranes and its therapeutic/diagnostic potential.

Indexed as

anticancer peptidedifferential scanning calorimetryDMPClangmuir minitroughMLVsRH-23

Identifiers

PMID36557189
PMCPMC9781852
OpenAlexW4312196222

What OpenQuestion holds

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LicenceCC BY
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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.