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...

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Main Authors: Alina Asandei, Andrei Ciuca, Aurelia Apetrei, Irina Schiopu, Loredana Mereuta, Chang Ho Seo, Yoonkyung Park, Tudor Luchian
Format: Article
Language:English
Published: Nature Publishing Group 2017-07-01
Series:Scientific Reports
Online Access:https://doi.org/10.1038/s41598-017-06435-1
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spelling doaj-680ddb1ae8bd43b6a3a45424a544db0f2020-12-08T00:50:19ZengNature Publishing GroupScientific Reports2045-23222017-07-017111310.1038/s41598-017-06435-1Nanoscale Investigation of Generation 1 PAMAM Dendrimers Interaction with a Protein NanoporeAlina Asandei0Andrei Ciuca1Aurelia Apetrei2Irina Schiopu3Loredana Mereuta4Chang Ho Seo5Yoonkyung Park6Tudor Luchian7Interdisciplinary Research Department, Alexandru I. Cuza UniversityDepartment of Physics, Alexandru I. Cuza UniversityDepartment of Physics, Alexandru I. Cuza UniversityInterdisciplinary Research Department, Alexandru I. Cuza UniversityDepartment of Physics, Alexandru I. Cuza UniversityDepartment of Bioinformatics, Kongju National UniversityDepartment of Department of Biomedical Science and Research Center for Proteinaceous Materials (RCPM), Chosun UniversityDepartment of Physics, Alexandru I. Cuza UniversityAbstract 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.https://doi.org/10.1038/s41598-017-06435-1
collection DOAJ
language English
format Article
sources DOAJ
author Alina Asandei
Andrei Ciuca
Aurelia Apetrei
Irina Schiopu
Loredana Mereuta
Chang Ho Seo
Yoonkyung Park
Tudor Luchian
spellingShingle 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
Scientific Reports
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 Publishing Group
series Scientific Reports
issn 2045-2322
publishDate 2017-07-01
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.
url https://doi.org/10.1038/s41598-017-06435-1
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