Source:http://linkedlifedata.com/resource/pubmed/id/11287091
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
2001-4-5
|
| pubmed:abstractText |
Neuropeptide Y (NPY) and pancreatic polypeptide (PP) bind to the Y-receptors with very different affinities: NPY has high affinity for the receptors Y(1), Y(2) and Y(5), while PP binds only to Y(4)-receptor with picomolar affinity. By exchanging of specific amino acid positions between the two peptides, we developed 38 full-length PP/NPY chimeras with binding properties that are completely different from those of the two native ligands. Pig NPY (pNPY) analogs containing the segment 19-23 from human PP (hPP) bound to the Y-receptors with much lower affinity than NPY itself. The affinity of the hPP analog containing the pNPY segments 1-7 and 19-23 was comparable to that of pNPY at the Y(1)- and Y(5)-receptor subtypes, and to that of hPP at the Y(4)-receptor. Furthermore, the presence of the segments 1-7 from chicken PP (cPP) and 19-23 from pNPY within the hPP sequence led to a ligand with IC(50) of 40 pM at the Y(5)-receptor. This is the most potent Y(5)-receptor ligand known so far, with 15-fold higher affinity than NPY.
|
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Mar
|
| pubmed:issn |
0196-9781
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
22
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
365-78
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11287091-Amino Acid Sequence,
pubmed-meshheading:11287091-Animals,
pubmed-meshheading:11287091-Binding, Competitive,
pubmed-meshheading:11287091-Cell Line,
pubmed-meshheading:11287091-Chickens,
pubmed-meshheading:11287091-Circular Dichroism,
pubmed-meshheading:11287091-Cricetinae,
pubmed-meshheading:11287091-Humans,
pubmed-meshheading:11287091-Inhibitory Concentration 50,
pubmed-meshheading:11287091-Kinetics,
pubmed-meshheading:11287091-Ligands,
pubmed-meshheading:11287091-Pancreatic Polypeptide,
pubmed-meshheading:11287091-Peptide Biosynthesis,
pubmed-meshheading:11287091-Protein Binding,
pubmed-meshheading:11287091-Rats,
pubmed-meshheading:11287091-Receptors, Neuropeptide Y,
pubmed-meshheading:11287091-Recombinant Fusion Proteins,
pubmed-meshheading:11287091-Sequence Homology, Amino Acid,
pubmed-meshheading:11287091-Structure-Activity Relationship,
pubmed-meshheading:11287091-Swine
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Y-receptor affinity modulation by the design of pancreatic polypeptide/neuropeptide Y chimera led to Y(5)-receptor ligands with picomolar affinity.
|
| pubmed:affiliation |
Department of Applied Bioscience, ETH Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|