Source:http://linkedlifedata.com/resource/pubmed/id/21106232
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2010-12-24
|
pubmed:abstractText |
To enhance the sensitivities and antigen-binding capacities of immunosensors, oriented immobilization of antibodies on the surface of the sensor chip is critical, but to date, this has not been adequately achieved. We describe a way of adsorbing immunoglobulin (Ig) proteins onto 32-nm bio-nanocapsules (BNCs) through IgG Fc-binding domains derived from Staphylococcus aureus protein A (ZZ-BNC). This arrangement permits approximately 60 molecules of mouse total IgG bind to ZZ-BNC and all the IgG Fv regions to be displayed outwardly for the effective binding of antigens. ZZ-BNCs adsorbed onto the gold surface of the sensor chip of the quartz crystal microbalance (QCM) could markedly enhance the sensitivity and antigen-binding capacity of the chip. On the sensor chip of surface plasmon resonance (SPR), antibodies on the ZZ-BNCs showed higher affinities to each antigen than those on protein A. The BNC-coated sensor chip is very stable, and should prove useful for various immunosensor applications due to oriented immobilization of antibodies.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
1878-5905
|
pubmed:author |
pubmed-author:ArakawaTakeshiT,
pubmed-author:ChoiEun KyungEK,
pubmed-author:HatahiraSatokoS,
pubmed-author:HinakoFumiyoF,
pubmed-author:HiramatsuShingoS,
pubmed-author:IijimaMasumiM,
pubmed-author:JeongSeong-YunSY,
pubmed-author:JungGimanG,
pubmed-author:JungJooheeJ,
pubmed-author:KadoyaHiroyasuH,
pubmed-author:KurodaShun'ichiS,
pubmed-author:KusunokiMasanobuM,
pubmed-author:MartinAaronA,
pubmed-author:NiimiTomoakiT,
pubmed-author:QuinnJohnJ,
pubmed-author:TanizawaKatsuyukiK,
pubmed-author:YoshimotoNobuoN
|
pubmed:copyrightInfo |
2010 Elsevier Ltd. All rights reserved.
|
pubmed:issnType |
Electronic
|
pubmed:volume |
32
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1455-64
|
pubmed:meshHeading |
pubmed-meshheading:21106232-Animals,
pubmed-meshheading:21106232-Biosensing Techniques,
pubmed-meshheading:21106232-Goats,
pubmed-meshheading:21106232-Humans,
pubmed-meshheading:21106232-Immunoglobulin Fc Fragments,
pubmed-meshheading:21106232-Immunoglobulin G,
pubmed-meshheading:21106232-Mice,
pubmed-meshheading:21106232-Microscopy, Atomic Force,
pubmed-meshheading:21106232-Microscopy, Electron, Transmission,
pubmed-meshheading:21106232-Nanocapsules,
pubmed-meshheading:21106232-Nanotechnology,
pubmed-meshheading:21106232-Rabbits,
pubmed-meshheading:21106232-Rats,
pubmed-meshheading:21106232-Sheep,
pubmed-meshheading:21106232-Staphylococcal Protein A,
pubmed-meshheading:21106232-Surface Plasmon Resonance
|
pubmed:year |
2011
|
pubmed:articleTitle |
Nanocapsules incorporating IgG Fc-binding domain derived from Staphylococcus aureus protein A for displaying IgGs on immunosensor chips.
|
pubmed:affiliation |
Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa 464-8601, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|