Linked Life Data

15656628

Source:http://linkedlifedata.com/resource/pubmed/id/15656628

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2005-1-19
pubmed:abstractText
A new concept of protein sensing at the air-water interface is introduced, based on amphiphilic receptor molecules embedded in a lipid monolayer. The process begins with incorporation of a small amount (0.13 equiv) of one or two different calix[4]arenes, adorned with charged functional groups at their upper rims, into a stearic acid monolayer. These doped monolayers are subsequently shown to attract peptides and proteins from the aqueous subphase. Depending on the host structure, the monolayers can be made selective for basic or acidic proteins. A working model is proposed, which explains the large observed p/A shifts with reincorporation of excess receptor molecules into the lipid monolayer after complex formation with the oppositely charged protein. This requires a self-assembly of multiple calixarene units over the protein surface, which bind the protein in a cooperative fashion. Oppositely charged calixarene derivatives do not form molecular capsules inside the monolayer, but rather remain separate inside the lipid layer, adopting a perpendicular orientation. They combine their hydrogen bond donor and acceptor capacities, and thus markedly enhance the sensitivity of the sensor system toward proteins, pushing the detection limits to 10 pM concentrations. The response pattern obtained from various receptor units inside the monolayer toward the same protein creates a fingerprint for this protein, which can hence be selectively detected at nanomolar concentrations (pattern recognition).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
904-15
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Nanomolar protein sensing with embedded receptor molecules.
pubmed:affiliation
The Philipps-Universität Marburg, Fachbereich Chemie, Hans-Meerwein-Strasse, 35032 Marburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't