Self-Assembly of Amphiphilic Dendrimers: The Role of Generation and Alkyl Chain Length in siRNA Interaction View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-09

AUTHORS

Valeria Márquez-Miranda, Ingrid Araya-Durán, María Belén Camarada, Jeffrey Comer, Jesús A Valencia-Gallegos, Fernando Danilo González-Nilo

ABSTRACT

An ideal nucleic-acid transfection system should combine the physical and chemical characteristics of cationic lipids and linear polymers to decrease cytotoxicity and uptake limitations. Previous research described new types of carriers termed amphiphilic dendrimers (ADs), which are based on polyamidoamine dendrimers (PAMAM). These ADs display the cell membrane affinity advantage of lipids and preserve the high affinity for DNA possessed by cationic dendrimers. These lipid/dendrimer hybrids consist of a low-generation, hydrophilic dendron (G2, G1, or G0) bonded to a hydrophobic tail. The G2-18C AD was reported to be an efficient siRNA vector with significant gene silencing. However, shorter tail ADs (G2-15C and G2-13C) and lower generation (G0 and G1) dendrimers failed as transfection carriers. To date, the self-assembly phenomenon of this class of amphiphilic dendrimers has not been molecularly explored using molecular simulation methods. To gain insight into these systems, the present study used coarse-grained molecular dynamics simulations to describe how ADs are able to self-assemble into an aggregate, and, specifically, how tail length and generation play a key role in this event. Finally, explanations are given for the better efficiency of G2/18-C as gene carrier in terms of binding of siRNA. This knowledge could be relevant for the design of novel, safer ADs with well-optimized affinity for siRNA. More... »

PAGES

29436

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep29436

DOI

http://dx.doi.org/10.1038/srep29436

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020820019

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27377641


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275 Universidad Andres Bello, Facultad de Biología, Center for Bioinformatics and Integrative Biology (CBIB), Av. República 239, Santiago, Chile.
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277 https://www.grid.ac/institutes/grid.419886.a schema:alternateName Monterrey Institute of Technology and Higher Education
278 schema:name Centro de Biotecnología FEMSA, Escuela de Ingeniería y Ciencias, Tecnológico de Monterrey, Av. Eugenio Garza Sada 2501 Sur, Col. Tecnológico, Monterrey, N.L, México.
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280 https://www.grid.ac/institutes/grid.440625.1 schema:alternateName Universidad Bernardo O'Higgins
281 schema:name Universidad Bernardo O Higgins, Laboratorio de Bionanotecnología, General Gana 1702, Santiago, Chile.
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283 https://www.grid.ac/institutes/grid.469835.5 schema:alternateName Fraunhofer Chile Research Foundation
284 schema:name Fundación Fraunhofer Chile Research, Las Condes, Chile.
285 Universidad Andres Bello, Facultad de Biología, Center for Bioinformatics and Integrative Biology (CBIB), Av. República 239, Santiago, Chile.
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