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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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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