Linked Life Data

17115927

Source:http://linkedlifedata.com/resource/pubmed/id/17115927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-11-22
pubmed:abstractText
The label-free RAPid 4 system that exploits resonant acoustic profiling (RAP) from Akubio (Cambridge, UK) was used to determine the affinity and kinetics for several different small molecule-receptor interactions. This was achieved by attaching the target receptor to the surface of quartz crystal resonators through a variety of specific coupling chemistries, followed by application of a small-molecular-weight ligand to the receptor via a microfluidic flow-based delivery system. Rank order of binding was determined for very weak interactions such as cofactor binding to glucose dehydrogenase. Moderate interaction affinities and binding kinetics could be determined for biotin binding to a specific antibody, and also for several low-molecular-weight sulfonamide analogues binding to human carbonic anhydrase isoform II. The equilibrium binding constants were in general agreement with the values obtained by kinetic analysis of the data, as well as with previously published values obtained using surface plasmon resonance, stopped flow fluorescence, and isothermal titration calorimetry.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1540-658X
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
565-73
pubmed:dateRevised
2007-12-3
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Quantification of small molecule-receptor affinities and kinetics by acoustic profiling.
pubmed:affiliation
Akubio Ltd., Cambridge, UK.
pubmed:publicationType
Journal Article, Evaluation Studies, Research Support, N.I.H., Extramural