Evidence map›Paper›PMID 36614022›Full record

ArticleInternational journal of molecular sciences2022

Understanding the Biophysical Interaction of LTX-315 with Tumoral Model Membranes.

Maria C Klaiss-Luna, Małgorzata Jemioła-Rzemińska, Kazimierz Strzałka, Marcela Manrique-Moreno

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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
1.1field-weighted citation impact, top 25% 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, 9 citations in OpenAlex.

  1. Article
  2. Immunobiological mechanisms of action of oncolytic peptides.Journal for immunotherapy of cancer · 2026
    Review
  3. Article
  4. Article
  5. Article
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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

4 authors at 2 institutions in 2 countries.

Maria C Klaiss-LunaChemistry Institute, Faculty of Exact and Natural Sciences, University of Antioquia, A.A 1226, Medellin 050010, Colombia.ORCID 0000-0002-0508-6486
Małgorzata Jemioła-RzemińskaFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-392 Krakow, Poland.ORCID 0000-0001-7790-4831
Kazimierz StrzałkaFaculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, 30-392 Krakow, Poland.ORCID 0000-0002-8367-4865
Marcela Manrique-MorenoChemistry Institute, Faculty of Exact and Natural Sciences, University of Antioquia, A.A 1226, Medellin 050010, Colombia.ORCID 0000-0002-2391-7343
Jagiellonian University · PLUniversidad de Antioquia · CO

Funding

European Regional Development Fund (contract No. POIG.02.01.00-12-167/08, Project Malopolska Centre of Biotechnology)Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University Statutory fundsMinisterio de Ciencia, Tecnología e Innovación - MinCiencias (Cod. 111584467189, RC 946-2019)
6 · The paper itself

Abstract

Host defense peptides are found primarily as natural antimicrobial agents among all lifeforms. These peptides and their synthetic derivatives have been extensively studied for their potential use as therapeutic agents. The most accepted mechanism of action of these peptides is related to a nonspecific mechanism associated with their interaction with the negatively charged groups present in membranes, inducing bilayer destabilization and cell death through several routes. Among the most recently reported peptides, LTX-315 has emerged as an important oncolytic peptide that is currently in several clinical trials against different cancer types. However, there is a lack of biophysical studies regarding LTX-315 and its interaction with membranes. This research focuses primarily on the understanding of the molecular bases of LTX-315's interaction with eukaryotic lipids, based on two artificial systems representative of non-tumoral and tumoral membranes. Additionally, the interaction with individual lipids was studied by differential scanning calorimetry and Fourier-transformed infrared spectroscopy. The results showed a strong interaction of LTX-315 with the negatively charged phosphatidylserine. The results are important for understanding and facilitating the design and development of improved peptides with anticancer activity.

Indexed as

Anti-Infective AgentsNeoplasmsAntimicrobial Cationic PeptidesHumansLipid BilayersLipidsMembranes, ArtificialOligopeptidesAnti-Infective AgentsAntimicrobial Cationic PeptidesLipid BilayersLipidsLTX-315Membranes, ArtificialOligopeptidesanticancer peptideslipid bilayerLTX-315model membranespeptide–membrane interaction

Identifiers

PMID36614022
PMCPMC9820754
OpenAlexW4313362569

What OpenQuestion holds

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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.