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

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 st...

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Autores:
Giordani Giordani, Cristiano
Russo, Stefano
Torrisi, Cristina
Morante, Silvia
Castelli, Francesco
Grazia Sarpietro, Maria
Tipo de recurso:
Article of investigation
Fecha de publicación:
2022
Institución:
Universidad de Antioquia
Repositorio:
Repositorio UdeA
Idioma:
eng
OAI Identifier:
oai:bibliotecadigital.udea.edu.co:10495/39538
Acceso en línea:
https://hdl.handle.net/10495/39538
Palabra clave:
Rastreo Diferencial de Calorimetría
Calorimetry, Differential Scanning
Dimiristoilfosfatidilcolina
Dimyristoylphosphatidylcholine
Péptidos
Peptides
Anticarcinógenos
Anticarcinogenic Agents
https://id.nlm.nih.gov/mesh/D002152
https://id.nlm.nih.gov/mesh/D004134
https://id.nlm.nih.gov/mesh/D010455
https://id.nlm.nih.gov/mesh/D016588
Rights
openAccess
License
http://creativecommons.org/licenses/by/2.5/co/
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dc.title.spa.fl_str_mv A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
title A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
spellingShingle A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
Rastreo Diferencial de Calorimetría
Calorimetry, Differential Scanning
Dimiristoilfosfatidilcolina
Dimyristoylphosphatidylcholine
Péptidos
Peptides
Anticarcinógenos
Anticarcinogenic Agents
https://id.nlm.nih.gov/mesh/D002152
https://id.nlm.nih.gov/mesh/D004134
https://id.nlm.nih.gov/mesh/D010455
https://id.nlm.nih.gov/mesh/D016588
title_short A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
title_full A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
title_fullStr A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
title_full_unstemmed A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
title_sort A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models
dc.creator.fl_str_mv Giordani Giordani, Cristiano
Russo, Stefano
Torrisi, Cristina
Morante, Silvia
Castelli, Francesco
Grazia Sarpietro, Maria
dc.contributor.author.none.fl_str_mv Giordani Giordani, Cristiano
Russo, Stefano
Torrisi, Cristina
Morante, Silvia
Castelli, Francesco
Grazia Sarpietro, Maria
dc.contributor.researchgroup.spa.fl_str_mv Productos Naturales Marinos
dc.subject.decs.none.fl_str_mv Rastreo Diferencial de Calorimetría
Calorimetry, Differential Scanning
Dimiristoilfosfatidilcolina
Dimyristoylphosphatidylcholine
Péptidos
Peptides
Anticarcinógenos
Anticarcinogenic Agents
topic Rastreo Diferencial de Calorimetría
Calorimetry, Differential Scanning
Dimiristoilfosfatidilcolina
Dimyristoylphosphatidylcholine
Péptidos
Peptides
Anticarcinógenos
Anticarcinogenic Agents
https://id.nlm.nih.gov/mesh/D002152
https://id.nlm.nih.gov/mesh/D004134
https://id.nlm.nih.gov/mesh/D010455
https://id.nlm.nih.gov/mesh/D016588
dc.subject.meshuri.none.fl_str_mv https://id.nlm.nih.gov/mesh/D002152
https://id.nlm.nih.gov/mesh/D004134
https://id.nlm.nih.gov/mesh/D010455
https://id.nlm.nih.gov/mesh/D016588
description 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.
publishDate 2022
dc.date.issued.none.fl_str_mv 2022
dc.date.accessioned.none.fl_str_mv 2024-06-01T21:07:14Z
dc.date.available.none.fl_str_mv 2024-06-01T21:07:14Z
dc.type.spa.fl_str_mv Artículo de investigación
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dc.identifier.citation.spa.fl_str_mv Giordani, C.; Russo, S.; Torrisi, C.; Morante, S.; Castelli, F.; Sarpietro, M.G. A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models. Membranes 2022, 12, 1282. https://doi.org/10.3390/10.3390/membranes12121282
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10495/39538
dc.identifier.doi.none.fl_str_mv 10.3390/membranes12121282
dc.identifier.eissn.none.fl_str_mv 2077-0375
identifier_str_mv Giordani, C.; Russo, S.; Torrisi, C.; Morante, S.; Castelli, F.; Sarpietro, M.G. A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models. Membranes 2022, 12, 1282. https://doi.org/10.3390/10.3390/membranes12121282
10.3390/membranes12121282
2077-0375
url https://hdl.handle.net/10495/39538
dc.language.iso.spa.fl_str_mv eng
language eng
dc.relation.ispartofjournalabbrev.spa.fl_str_mv Membranes
dc.relation.citationendpage.spa.fl_str_mv 14
dc.relation.citationissue.spa.fl_str_mv 12
dc.relation.citationstartpage.spa.fl_str_mv 1
dc.relation.citationvolume.spa.fl_str_mv 12
dc.relation.ispartofjournal.spa.fl_str_mv Membranes
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dc.format.extent.spa.fl_str_mv 14 páginas
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dc.publisher.place.spa.fl_str_mv Basilea, Suiza
institution Universidad de Antioquia
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spelling Giordani Giordani, CristianoRusso, StefanoTorrisi, CristinaMorante, SilviaCastelli, FrancescoGrazia Sarpietro, MariaProductos Naturales Marinos2024-06-01T21:07:14Z2024-06-01T21:07:14Z2022Giordani, C.; Russo, S.; Torrisi, C.; Morante, S.; Castelli, F.; Sarpietro, M.G. A Thermodynamic Study on the Interaction between RH-23 Peptide and DMPC-Based Biomembrane Models. Membranes 2022, 12, 1282. https://doi.org/10.3390/10.3390/membranes12121282https://hdl.handle.net/10495/3953810.3390/membranes121212822077-0375ABSTRACT: 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.Universidad de Antioquia. 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