Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels
Incorporation of biological systems in water nanodroplets has recently emerged as a new frontier to investigate structural changes of biomolecules, with perspective applications in ultra-fast drug delivery. We report on the molecular dynamics of the digestive protein Pepsin subjected to a double con...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2019-06-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/20/12/2965 |
id |
doaj-5a219b2e35084a68bfbcc5a10a2671ac |
---|---|
record_format |
Article |
spelling |
doaj-5a219b2e35084a68bfbcc5a10a2671ac2020-11-25T02:22:46ZengMDPI AGInternational Journal of Molecular Sciences1422-00672019-06-012012296510.3390/ijms20122965ijms20122965Confining a Protein-Containing Water Nanodroplet inside Silica NanochannelsLara Giussani0Gloria Tabacchi1Salvatore Coluccia2Ettore Fois3Dipartimento di Scienza e Alta Tecnologia and INSTM udr Como, Insubria University, Via Valleggio 9, I-22100 Como, ItalyDipartimento di Scienza e Alta Tecnologia and INSTM udr Como, Insubria University, Via Valleggio 9, I-22100 Como, ItalyDipartimento di Chimica, Turin University, Via P. Giuria 7, I-10125 Turin, ItalyDipartimento di Scienza e Alta Tecnologia and INSTM udr Como, Insubria University, Via Valleggio 9, I-22100 Como, ItalyIncorporation of biological systems in water nanodroplets has recently emerged as a new frontier to investigate structural changes of biomolecules, with perspective applications in ultra-fast drug delivery. We report on the molecular dynamics of the digestive protein Pepsin subjected to a double confinement. The double confinement stemmed from embedding the protein inside a water nanodroplet, which in turn was caged in a nanochannel mimicking the mesoporous silica SBA-15. The nano-bio-droplet, whose size fits with the pore diameter, behaved differently depending on the protonation state of the pore surface silanols. Neutral channel sections allowed for the droplet to flow, while deprotonated sections acted as anchoring piers for the droplet. Inside the droplet, the protein, not directly bonded to the surface, showed a behavior similar to that reported for bulk water solutions, indicating that double confinement should not alter its catalytic activity. Our results suggest that nanobiodroplets, recently fabricated in volatile environments, can be encapsulated and stored in mesoporous silicas.https://www.mdpi.com/1422-0067/20/12/2965host–guest systemsprotein confinementmolecular dynamicsmesoporous silicawater nanodroplets |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lara Giussani Gloria Tabacchi Salvatore Coluccia Ettore Fois |
spellingShingle |
Lara Giussani Gloria Tabacchi Salvatore Coluccia Ettore Fois Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels International Journal of Molecular Sciences host–guest systems protein confinement molecular dynamics mesoporous silica water nanodroplets |
author_facet |
Lara Giussani Gloria Tabacchi Salvatore Coluccia Ettore Fois |
author_sort |
Lara Giussani |
title |
Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels |
title_short |
Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels |
title_full |
Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels |
title_fullStr |
Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels |
title_full_unstemmed |
Confining a Protein-Containing Water Nanodroplet inside Silica Nanochannels |
title_sort |
confining a protein-containing water nanodroplet inside silica nanochannels |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2019-06-01 |
description |
Incorporation of biological systems in water nanodroplets has recently emerged as a new frontier to investigate structural changes of biomolecules, with perspective applications in ultra-fast drug delivery. We report on the molecular dynamics of the digestive protein Pepsin subjected to a double confinement. The double confinement stemmed from embedding the protein inside a water nanodroplet, which in turn was caged in a nanochannel mimicking the mesoporous silica SBA-15. The nano-bio-droplet, whose size fits with the pore diameter, behaved differently depending on the protonation state of the pore surface silanols. Neutral channel sections allowed for the droplet to flow, while deprotonated sections acted as anchoring piers for the droplet. Inside the droplet, the protein, not directly bonded to the surface, showed a behavior similar to that reported for bulk water solutions, indicating that double confinement should not alter its catalytic activity. Our results suggest that nanobiodroplets, recently fabricated in volatile environments, can be encapsulated and stored in mesoporous silicas. |
topic |
host–guest systems protein confinement molecular dynamics mesoporous silica water nanodroplets |
url |
https://www.mdpi.com/1422-0067/20/12/2965 |
work_keys_str_mv |
AT laragiussani confiningaproteincontainingwaternanodropletinsidesilicananochannels AT gloriatabacchi confiningaproteincontainingwaternanodropletinsidesilicananochannels AT salvatorecoluccia confiningaproteincontainingwaternanodropletinsidesilicananochannels AT ettorefois confiningaproteincontainingwaternanodropletinsidesilicananochannels |
_version_ |
1724861771868536832 |