Linked Life Data

11015207

Source:http://linkedlifedata.com/resource/pubmed/id/11015207

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2000-11-1
pubmed:abstractText
We report the synthesis of a new integrin alpha(IIb)beta(3)-specific cyclic hexapeptide that contains an Arg-Gly-Asp (RGD) sequence and is coupled to a dimyristoylthioglyceryl anchor. We demonstrate that this ligand is useful to study specific integrin binding to membrane surfaces. With the help of biotinylated analogues of the peptide, a spacer of optimal length between the peptide and lipid moieties was searched for by evaluating the binding strength with an enzyme-coupled immunosorbent assay (ELISA) and by surface plasmon resonance (SPR). It was found to be strongly dependent on the length of the spacer introduced between the biotin and peptide moieties of the ligands, which consisted either of epsilon-aminohexanoic acid (epsilonAhx) or of epsilonAhx with two additional glycine units. Best results were obtained with c[Arg-Gly-Asp-D-Phe-Lys(Biot-Ahx-Gly-Gly)-Gly-] with dissociation constants of K(D) = 0.158 microM from ELISA and K(D) = 1.1 microM from SPR measurements. The analogous lipopeptide, c[Arg-Gly-Asp-D-Phe-Lys([dimyristoyl-3-thioglyceryl-succinimido -propanoyl]Ahx-Gly-Gly)-Gly], was used as a membrane-anchored integrin ligand. It is shown by fluorescence microscopy and cryo electron microscopy that integrin reconstituted into phospholipid vesicles binds to vesicles decorated with the lipopeptide, forming regularly spaced bridges between the two kinds of vesicles. The novel integrin-specific ligand allows establishment of new model systems for systematic studies of the self-organization of integrin clusters and focal adhesion complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12284-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11015207-Binding Sites, pubmed-meshheading:11015207-Calorimetry, Differential Scanning, pubmed-meshheading:11015207-Cell Adhesion, pubmed-meshheading:11015207-Cryoelectron Microscopy, pubmed-meshheading:11015207-Dimyristoylphosphatidylcholine, pubmed-meshheading:11015207-Humans, pubmed-meshheading:11015207-Kinetics, pubmed-meshheading:11015207-Lipid Bilayers, pubmed-meshheading:11015207-Lipoproteins, pubmed-meshheading:11015207-Microscopy, Confocal, pubmed-meshheading:11015207-Microscopy, Fluorescence, pubmed-meshheading:11015207-Models, Biological, pubmed-meshheading:11015207-Oligopeptides, pubmed-meshheading:11015207-Peptides, Cyclic, pubmed-meshheading:11015207-Phosphatidylglycerols, pubmed-meshheading:11015207-Photomicrography, pubmed-meshheading:11015207-Platelet Glycoprotein GPIIb-IIIa Complex
pubmed:year
2000
pubmed:articleTitle
Intervesicle cross-linking with integrin alpha IIb beta 3 and cyclic-RGD-lipopeptide. A model of cell-adhesion processes.
pubmed:affiliation
Physik-Department E 22 and Institut für Organische Chemie und Biochemie, Technische Universität München, D-85747 Garching, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't