Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore

Abstract Herein, we describe at uni-molecular level the interactions between poly(amidoamine) (PAMAM) dendrimers of generation 1 and the α-hemolysin protein nanopore, at acidic and neutral pH, and ionic strengths of 0.5 M and 1 M KCl, via single-molecule electrical recordings. The results indicate t...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Alina Asandei, Andrei Ciuca, Aurelia Apetrei, Irina Schiopu, Loredana Mereuta, Chang Ho Seo, Yoonkyung Park, Tudor Luchian
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/680ddb1ae8bd43b6a3a45424a544db0f
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:680ddb1ae8bd43b6a3a45424a544db0f
record_format	dspace
spelling	oai:doaj.org-article:680ddb1ae8bd43b6a3a45424a544db0f2021-12-02T16:06:18ZNanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore10.1038/s41598-017-06435-12045-2322https://doaj.org/article/680ddb1ae8bd43b6a3a45424a544db0f2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06435-1https://doaj.org/toc/2045-2322Abstract Herein, we describe at uni-molecular level the interactions between poly(amidoamine) (PAMAM) dendrimers of generation 1 and the α-hemolysin protein nanopore, at acidic and neutral pH, and ionic strengths of 0.5 M and 1 M KCl, via single-molecule electrical recordings. The results indicate that kinetics of dendrimer-α-hemolysin reversible interactions is faster at neutral as compared to acidic pH, and we propose as a putative explanation the fine interplay among conformational and rigidity changes on the dendrimer structure, and the ionization state of the dendrimer and the α-hemolysin. From the analysis of the dendrimer’s residence time inside the nanopore, we posit that the pH- and salt-dependent, long-range electrostatic interactions experienced by the dendrimer inside the ion-selective α-hemolysin, induce a non-Stokesian diffusive behavior of the analyte inside the nanopore. We also show that the ability of dendrimer molecules to adapt their structure to nanoscopic spaces, and control the flow of matter through the α-hemolysin nanopore, depends non-trivially on the pH- and salt-induced conformational changes of the dendrimer.Alina AsandeiAndrei CiucaAurelia ApetreiIrina SchiopuLoredana MereutaChang Ho SeoYoonkyung ParkTudor LuchianNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alina Asandei Andrei Ciuca Aurelia Apetrei Irina Schiopu Loredana Mereuta Chang Ho Seo Yoonkyung Park Tudor Luchian Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
description	Abstract Herein, we describe at uni-molecular level the interactions between poly(amidoamine) (PAMAM) dendrimers of generation 1 and the α-hemolysin protein nanopore, at acidic and neutral pH, and ionic strengths of 0.5 M and 1 M KCl, via single-molecule electrical recordings. The results indicate that kinetics of dendrimer-α-hemolysin reversible interactions is faster at neutral as compared to acidic pH, and we propose as a putative explanation the fine interplay among conformational and rigidity changes on the dendrimer structure, and the ionization state of the dendrimer and the α-hemolysin. From the analysis of the dendrimer’s residence time inside the nanopore, we posit that the pH- and salt-dependent, long-range electrostatic interactions experienced by the dendrimer inside the ion-selective α-hemolysin, induce a non-Stokesian diffusive behavior of the analyte inside the nanopore. We also show that the ability of dendrimer molecules to adapt their structure to nanoscopic spaces, and control the flow of matter through the α-hemolysin nanopore, depends non-trivially on the pH- and salt-induced conformational changes of the dendrimer.
format	article
author	Alina Asandei Andrei Ciuca Aurelia Apetrei Irina Schiopu Loredana Mereuta Chang Ho Seo Yoonkyung Park Tudor Luchian
author_facet	Alina Asandei Andrei Ciuca Aurelia Apetrei Irina Schiopu Loredana Mereuta Chang Ho Seo Yoonkyung Park Tudor Luchian
author_sort	Alina Asandei
title	Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
title_short	Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
title_full	Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
title_fullStr	Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
title_full_unstemmed	Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore
title_sort	nanoscale investigation of generation 1 pamam dendrimers interaction with a protein nanopore
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/680ddb1ae8bd43b6a3a45424a544db0f
work_keys_str_mv	AT alinaasandei nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT andreiciuca nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT aureliaapetrei nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT irinaschiopu nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT loredanamereuta nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT changhoseo nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT yoonkyungpark nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore AT tudorluchian nanoscaleinvestigationofgeneration1pamamdendrimersinteractionwithaproteinnanopore
_version_	1718385029442174976

Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein Nanopore

Ejemplares similares