Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface
Functionalization of nanoparticles surfaces have been widely used to improve diagnostic and therapeutic biological outcome. Several methods can be applied to modify nanoparticle surface; however, in this article we focus toward a simple and less time-consuming method. We applied an adsorption method...
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MDPI AG
2022-04-01
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author | Sara Silva Joana Marto Lídia M. Gonçalves Henrique S. Fernandes Sérgio F. Sousa António J. Almeida Nuno Vale |
author_facet | Sara Silva Joana Marto Lídia M. Gonçalves Henrique S. Fernandes Sérgio F. Sousa António J. Almeida Nuno Vale |
author_sort | Sara Silva |
collection | DOAJ |
description | Functionalization of nanoparticles surfaces have been widely used to improve diagnostic and therapeutic biological outcome. Several methods can be applied to modify nanoparticle surface; however, in this article we focus toward a simple and less time-consuming method. We applied an adsorption method on already formulated nanostructured lipid carriers (NLC) to functionalize these nanoparticles with three distinct peptides sequences. We selected a cell-penetrating peptide (CPP), a lysine modified model amphipathic peptide (Lys(N<sub>3</sub>)-MAP), CPP/drug complex, and the neuropeptide Y. The aim of this work is to evaluate the effect of several parameters such as peptide concentration, different types of NLC, different types of peptides, and incubation medium on the physicochemical proprieties of NLC and determine if adsorption occurs. The preliminary results from zeta potential analysis indicate some evidence that this method was successful in adsorbing three types of peptides onto NLC. Several non-covalent interactions appear to be involved in peptide adsorption with the possibility of three adsorption peptide hypothesis that may occur with NLC in solution. Moreover, and for the first time, in silico docking analysis demonstrated strong interaction between CPP MAP and NPY Y1 receptor with high score values when compared to standard antagonist and NPY. |
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publishDate | 2022-04-01 |
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spelling | doaj.art-e09f01db57034557aac25fcaf71887bd2023-11-23T08:48:57ZengMDPI AGMolecules1420-30492022-04-01279273410.3390/molecules27092734Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle SurfaceSara Silva0Joana Marto1Lídia M. Gonçalves2Henrique S. Fernandes3Sérgio F. Sousa4António J. Almeida5Nuno Vale6OncoPharma Research Group, Center for Health Technology and Services Research (CINTESIS), Rua Dr. Plácido da Costa, 4200-450 Porto, PortugalResearch Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, PortugalResearch Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, PortugalUCIBIO/REQUIMTE, BioSIM, Departamento de Medicina, Faculdade de Medicina da Universidade Do Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalUCIBIO/REQUIMTE, BioSIM, Departamento de Medicina, Faculdade de Medicina da Universidade Do Porto, Alameda Prof. Hernâni Monteiro, 4200-319 Porto, PortugalResearch Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, PortugalOncoPharma Research Group, Center for Health Technology and Services Research (CINTESIS), Rua Dr. Plácido da Costa, 4200-450 Porto, PortugalFunctionalization of nanoparticles surfaces have been widely used to improve diagnostic and therapeutic biological outcome. Several methods can be applied to modify nanoparticle surface; however, in this article we focus toward a simple and less time-consuming method. We applied an adsorption method on already formulated nanostructured lipid carriers (NLC) to functionalize these nanoparticles with three distinct peptides sequences. We selected a cell-penetrating peptide (CPP), a lysine modified model amphipathic peptide (Lys(N<sub>3</sub>)-MAP), CPP/drug complex, and the neuropeptide Y. The aim of this work is to evaluate the effect of several parameters such as peptide concentration, different types of NLC, different types of peptides, and incubation medium on the physicochemical proprieties of NLC and determine if adsorption occurs. The preliminary results from zeta potential analysis indicate some evidence that this method was successful in adsorbing three types of peptides onto NLC. Several non-covalent interactions appear to be involved in peptide adsorption with the possibility of three adsorption peptide hypothesis that may occur with NLC in solution. Moreover, and for the first time, in silico docking analysis demonstrated strong interaction between CPP MAP and NPY Y1 receptor with high score values when compared to standard antagonist and NPY.https://www.mdpi.com/1420-3049/27/9/2734cell-penetrating peptideneuropeptide Ynanoparticlesadsorptionpotential zetaTacrine |
spellingShingle | Sara Silva Joana Marto Lídia M. Gonçalves Henrique S. Fernandes Sérgio F. Sousa António J. Almeida Nuno Vale Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface Molecules cell-penetrating peptide neuropeptide Y nanoparticles adsorption potential zeta Tacrine |
title | Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface |
title_full | Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface |
title_fullStr | Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface |
title_full_unstemmed | Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface |
title_short | Development of Neuropeptide Y and Cell-Penetrating Peptide MAP Adsorbed onto Lipid Nanoparticle Surface |
title_sort | development of neuropeptide y and cell penetrating peptide map adsorbed onto lipid nanoparticle surface |
topic | cell-penetrating peptide neuropeptide Y nanoparticles adsorption potential zeta Tacrine |
url | https://www.mdpi.com/1420-3049/27/9/2734 |
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