File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Using polymer conformation to control architecture in semiconducting polymer/viral capsid assemblies

TitleUsing polymer conformation to control architecture in semiconducting polymer/viral capsid assemblies
Authors
Issue Date2011
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/ancac3/index.html
Citation
ACS Nano, 2011, v. 5 n. 10, p. 7730-7738 How to Cite?
AbstractCowpea chlorotic mottle virus is a single-stranded RNA plant virus with a diameter of 28 nm. The proteins comprising the capsid of this virus can be purified and reassembled either by themselves to form hollow structures or with polyanions such as double-stranded DNA or single-stranded RNA. Depending on pH and ionic strength, a diverse range of structures and shapes can form. The work presented here focuses on using these proteins to encapsulate a fluorescent polyanionic semiconducting polymer, MPS-PPV (poly-2-methoxy-5-propyloxy sulfonate phenylene vinlyene), in order to obtain optically active virus-like particles. After encapsulation, fluorescence from MPS-PPV shows two distinct peaks, which suggests the polymer may be in two conformations. A combination of TEM, fluorescence anisotropy, and sucrose gradient separation indicate that the blue peak arises from polymer encapsulated into spherical particles, while the redder peak corresponds to polymers contained in rod-like cages. Ionic strength during assembly can be used to tune the propensity to form rods or spheres. The results illustrate the synergy of hybrid synthetic/biological systems: polymer conformation drives the structure of this composite material, which in turn modifies the polymer optical properties. This synergy could be useful for the future development of synthetic/biological hybrid materials with designated functionality.
Persistent Identifierhttp://hdl.handle.net/10722/177561
ISSN
2015 Impact Factor: 13.334
2015 SCImago Journal Rankings: 7.120
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorNg, BCHen_US
dc.contributor.authorChan, STen_US
dc.contributor.authorLin, Jen_US
dc.contributor.authorTolbert, SHen_US
dc.date.accessioned2012-12-18T05:26:54Z-
dc.date.available2012-12-18T05:26:54Z-
dc.date.issued2011en_US
dc.identifier.citationACS Nano, 2011, v. 5 n. 10, p. 7730-7738en_US
dc.identifier.issn1936-0851en_US
dc.identifier.urihttp://hdl.handle.net/10722/177561-
dc.description.abstractCowpea chlorotic mottle virus is a single-stranded RNA plant virus with a diameter of 28 nm. The proteins comprising the capsid of this virus can be purified and reassembled either by themselves to form hollow structures or with polyanions such as double-stranded DNA or single-stranded RNA. Depending on pH and ionic strength, a diverse range of structures and shapes can form. The work presented here focuses on using these proteins to encapsulate a fluorescent polyanionic semiconducting polymer, MPS-PPV (poly-2-methoxy-5-propyloxy sulfonate phenylene vinlyene), in order to obtain optically active virus-like particles. After encapsulation, fluorescence from MPS-PPV shows two distinct peaks, which suggests the polymer may be in two conformations. A combination of TEM, fluorescence anisotropy, and sucrose gradient separation indicate that the blue peak arises from polymer encapsulated into spherical particles, while the redder peak corresponds to polymers contained in rod-like cages. Ionic strength during assembly can be used to tune the propensity to form rods or spheres. The results illustrate the synergy of hybrid synthetic/biological systems: polymer conformation drives the structure of this composite material, which in turn modifies the polymer optical properties. This synergy could be useful for the future development of synthetic/biological hybrid materials with designated functionality.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/ancac3/index.htmlen_US
dc.relation.ispartofACS Nanoen_US
dc.subject.meshBromovirus - chemistry-
dc.subject.meshCapsid - chemistry-
dc.subject.meshMolecular conformation-
dc.subject.meshPolyvinyls - chemistry-
dc.subject.meshSemiconductors - virology-
dc.titleUsing polymer conformation to control architecture in semiconducting polymer/viral capsid assembliesen_US
dc.typeArticleen_US
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1936-0851&volume=5&issue=10&spage=7730&epage=7738&date=2011&atitle=Using+polymer+conformation+to+control+architecture+in+semiconducting+polymer/viral+capsid+assembliesen_US
dc.identifier.emailNg, BCH: ngbenny@hku.hken_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1021/nn202493wen_US
dc.identifier.pmid21942298-
dc.identifier.pmcidPMC3215919-
dc.identifier.scopuseid_2-s2.0-80055012215-
dc.identifier.hkuros202531en_US
dc.identifier.volume5en_US
dc.identifier.issue10en_US
dc.identifier.spage7730en_US
dc.identifier.epage7738en_US
dc.identifier.isiWOS:000296208700018-
dc.publisher.placeUnited States-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats