File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Preparation of supported lipid membranes for aquaporin Z incorporation

TitlePreparation of supported lipid membranes for aquaporin Z incorporation
Authors
Issue Date2012
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/colsurfb
Citation
Colloids And Surfaces B: Biointerfaces, 2012, v. 94, p. 333-340 How to Cite?
AbstractThere has been a recent surge of interest to mimic the performance of natural cellular membranes by incorporating water channel proteins-aquaporins (AQPs) into various ultrathin films for water filtration applications. To make biomimetic membranes one of the most crucial steps is preparing a defect-free platform for AQPs incorporation on a suitable substrate. In this study two methods were used to prepare supported lipid membranes on NF membrane surfaces under a benign pH condition of 7.8. One method was direct vesicle fusion on a hydrophilic membrane NF-270; the other was vesicle fusion facilitated by hydraulic pressure on a modified hydrophilic NF-270 membrane whose surface has been spin-coated with positively charged lipids. Experiments revealed that the supported lipid membrane without AQPs prepared by the spin coating plus vesicle fusion had a much lower defect density than that prepared by vesicle fusion alone. It appears that the surface roughness and charge are the main factors determining the quality of the supported lipid membrane. Aquaporin Z (AqpZ) proteins were successfully incorporated into 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) liposomes and its permeability was measured by the stopped-flow experimental procedure. However, after the proteoliposomes have been fused onto the modified substrate, the AqpZ function in the resultant membrane was not observed and AFM images showed distinct aggregations of unfused proteoliposomes or AqpZ proteins on the substrate surface. It is speculated that the inhibition of AqpZ function may be caused by the low lipid mobility on the NF membrane surface. Further investigations to evaluate and optimize the structure-performance relationship are required. © 2012 Elsevier B.V.
Persistent Identifierhttp://hdl.handle.net/10722/185424
ISSN
2015 Impact Factor: 3.902
2015 SCImago Journal Rankings: 1.105
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLi, Xen_US
dc.contributor.authorWang, Ren_US
dc.contributor.authorTang, Cen_US
dc.contributor.authorVararattanavech, Aen_US
dc.contributor.authorZhao, Yen_US
dc.contributor.authorTorres, Jen_US
dc.contributor.authorFane, Ten_US
dc.date.accessioned2013-07-30T07:32:25Z-
dc.date.available2013-07-30T07:32:25Z-
dc.date.issued2012en_US
dc.identifier.citationColloids And Surfaces B: Biointerfaces, 2012, v. 94, p. 333-340en_US
dc.identifier.issn0927-7765en_US
dc.identifier.urihttp://hdl.handle.net/10722/185424-
dc.description.abstractThere has been a recent surge of interest to mimic the performance of natural cellular membranes by incorporating water channel proteins-aquaporins (AQPs) into various ultrathin films for water filtration applications. To make biomimetic membranes one of the most crucial steps is preparing a defect-free platform for AQPs incorporation on a suitable substrate. In this study two methods were used to prepare supported lipid membranes on NF membrane surfaces under a benign pH condition of 7.8. One method was direct vesicle fusion on a hydrophilic membrane NF-270; the other was vesicle fusion facilitated by hydraulic pressure on a modified hydrophilic NF-270 membrane whose surface has been spin-coated with positively charged lipids. Experiments revealed that the supported lipid membrane without AQPs prepared by the spin coating plus vesicle fusion had a much lower defect density than that prepared by vesicle fusion alone. It appears that the surface roughness and charge are the main factors determining the quality of the supported lipid membrane. Aquaporin Z (AqpZ) proteins were successfully incorporated into 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) liposomes and its permeability was measured by the stopped-flow experimental procedure. However, after the proteoliposomes have been fused onto the modified substrate, the AqpZ function in the resultant membrane was not observed and AFM images showed distinct aggregations of unfused proteoliposomes or AqpZ proteins on the substrate surface. It is speculated that the inhibition of AqpZ function may be caused by the low lipid mobility on the NF membrane surface. Further investigations to evaluate and optimize the structure-performance relationship are required. © 2012 Elsevier B.V.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/colsurfben_US
dc.relation.ispartofColloids and Surfaces B: Biointerfacesen_US
dc.subject.meshAquaporins - Chemistryen_US
dc.subject.meshBiomimetic Materials - Chemical Synthesisen_US
dc.subject.meshEscherichia Coli Proteins - Chemistryen_US
dc.subject.meshFiltrationen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMembrane Fusionen_US
dc.subject.meshMicroscopy, Atomic Forceen_US
dc.subject.meshPermeabilityen_US
dc.subject.meshPhosphatidylcholines - Chemistryen_US
dc.subject.meshProteolipids - Chemistryen_US
dc.subject.meshStatic Electricityen_US
dc.subject.meshSurface Propertiesen_US
dc.subject.meshWater Purificationen_US
dc.titlePreparation of supported lipid membranes for aquaporin Z incorporationen_US
dc.typeArticleen_US
dc.identifier.emailTang, C: tangc@hku.hken_US
dc.identifier.authorityTang, C=rp01765en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.colsurfb.2012.02.013en_US
dc.identifier.pmid22386862-
dc.identifier.scopuseid_2-s2.0-84862810113en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-84862810113&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume94en_US
dc.identifier.spage333en_US
dc.identifier.epage340en_US
dc.identifier.isiWOS:000302979900048-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridLi, X=55262333500en_US
dc.identifier.scopusauthoridWang, R=35081334000en_US
dc.identifier.scopusauthoridTang, C=35489259800en_US
dc.identifier.scopusauthoridVararattanavech, A=23986850300en_US
dc.identifier.scopusauthoridZhao, Y=8579132600en_US
dc.identifier.scopusauthoridTorres, J=55323863800en_US
dc.identifier.scopusauthoridFane, T=55261398300en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats