Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein
Understanding of self-assembly mechanism of viruslike protein cage is important in controlling release of molecular cargo for applications in drug delivery. E2 core protein is composed of 60 subunits which self-assemble into a hollow 25-nm porous protein cage. Due to its virus like dodecahedral stru...
Saved in:
Main Authors: | , , , |
---|---|
Other Authors: | |
Format: | Conference or Workshop Item |
Language: | English |
Published: |
2013
|
Online Access: | https://hdl.handle.net/10356/96087 http://hdl.handle.net/10220/10105 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
id |
sg-ntu-dr.10356-96087 |
---|---|
record_format |
dspace |
spelling |
sg-ntu-dr.10356-960872023-12-29T06:44:16Z Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein Peng, Tao Tan, Sze Wah Dharmawan, Ratna Ekawati Lim, Sierin School of Chemical and Biomedical Engineering International Conference on Nanotechnology - Research and Commercialization (2011 : Sabah, Malaysia) Understanding of self-assembly mechanism of viruslike protein cage is important in controlling release of molecular cargo for applications in drug delivery. E2 core protein is composed of 60 subunits which self-assemble into a hollow 25-nm porous protein cage. Due to its virus like dodecahedral structure without infectious capacity, we are interested in its potential application as nanocapsule in drug delivery. In our study, extrinsic and intrinsic factors that influence self-assembly were evaluated. Extrinsic factors, such as salts and denaturants, were introduced into E2 protein solution. The hydrodynamic diameter of the E2 core protein was used to monitor its disassembly or aggregation. We found that the protein size increased proportionally with the salt concentration while the size decreased as the denaturant concentration increased. To assess intrinsic factors that influence E2 self-assembly, we identified some key amino acids at interfaces of subunits and performed site-directed mutagenesis on them. Characterizations of each mutant for size and secondary structure contents were performed. We found that mutations at the inner surface have no apparent effects on both protein sizes and secondary structures. The mutations at intra-trimer interfaces changed the secondary structure contents but the protein sizes remained stable. Published version 2013-06-10T03:56:35Z 2019-12-06T19:25:25Z 2013-06-10T03:56:35Z 2019-12-06T19:25:25Z 2012 2012 Conference Paper Peng, T., Tan, S. W., Dharmawan, R. E., & Lim, S. (2012). Investigating the Influence of Ionic Concentrations and Subunit Interactions on the Self-Assembly of E2 Protein. International Conference on Nanotechnology - Research and Commercialization 2011, 1502, 34-52. https://hdl.handle.net/10356/96087 http://hdl.handle.net/10220/10105 10.1063/1.4769132 en © 2012 American Institute of Physics. This paper was published in International Conference on Nanotechnology - Research and Commercialization 2011 and is made available as an electronic reprint (preprint) with permission of American Institute of Physics. The paper can be found at the following official DOI: [http://dx.doi.org/10.1063/1.4769132]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf |
institution |
Nanyang Technological University |
building |
NTU Library |
continent |
Asia |
country |
Singapore Singapore |
content_provider |
NTU Library |
collection |
DR-NTU |
language |
English |
description |
Understanding of self-assembly mechanism of viruslike protein cage is important in controlling release of molecular cargo for applications in drug delivery. E2 core protein is composed of 60 subunits which self-assemble into a hollow 25-nm porous protein cage. Due to its virus like dodecahedral structure without infectious capacity, we are interested in its potential application as nanocapsule in drug delivery. In our study, extrinsic and intrinsic factors that influence self-assembly were evaluated. Extrinsic factors, such as salts and denaturants, were introduced into E2 protein solution. The hydrodynamic diameter of the E2 core protein was used to monitor its disassembly or aggregation. We found that the protein size increased proportionally with the salt concentration while the size decreased as the denaturant concentration increased. To assess intrinsic factors that influence E2 self-assembly, we identified some key amino acids at interfaces of subunits and performed site-directed mutagenesis on them. Characterizations of each mutant for size and secondary structure contents were performed. We found that mutations at the inner surface have no apparent effects on both protein sizes and secondary structures. The mutations at intra-trimer interfaces changed the secondary structure contents but the protein sizes remained stable. |
author2 |
School of Chemical and Biomedical Engineering |
author_facet |
School of Chemical and Biomedical Engineering Peng, Tao Tan, Sze Wah Dharmawan, Ratna Ekawati Lim, Sierin |
format |
Conference or Workshop Item |
author |
Peng, Tao Tan, Sze Wah Dharmawan, Ratna Ekawati Lim, Sierin |
spellingShingle |
Peng, Tao Tan, Sze Wah Dharmawan, Ratna Ekawati Lim, Sierin Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
author_sort |
Peng, Tao |
title |
Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
title_short |
Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
title_full |
Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
title_fullStr |
Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
title_full_unstemmed |
Investigating the influence of ionic concentrations and subunit interactions on the self-assembly of E2 protein |
title_sort |
investigating the influence of ionic concentrations and subunit interactions on the self-assembly of e2 protein |
publishDate |
2013 |
url |
https://hdl.handle.net/10356/96087 http://hdl.handle.net/10220/10105 |
_version_ |
1787136776011251712 |