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  Intervesicle cross-linking with integrin alpha(IIb)beta(3) and cyclic-RGD-lipopeptide. A model of cell-adhesion processes

Hu, B., Finsinger, D., Peter, K., Guttenberg, Z., Bärmann, M., Kessler, I., et al. (2000). Intervesicle cross-linking with integrin alpha(IIb)beta(3) and cyclic-RGD-lipopeptide. A model of cell-adhesion processes. Biochemistry, 39(40), 12284-12294.

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Genre: Journal Article
Alternative Title : Biochemistry

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Hu, B., Author
Finsinger, D., Author
Peter, K., Author
Guttenberg, Z., Author
Bärmann, M., Author
Kessler, I., Author
Escherich, A.1, Author              
Moroder, L.1, Author              
Böhm, J.1, Author              
Baumeister, W.1, Author              
Sui, S. F., Author
Sackmann, E., Author
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1External Organizations, ou_persistent22              

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Free keywords: Iib-iiia complex; Fibrinogen binding; Molecular architecture; Glycoprotein iib/iiia; Signal-transduction; Electron-microscopy; Peptide-amphiphiles; Membrane; Recognition; Protein.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: 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 E-aminohexanoic acid (epsilon Ahx) or of epsilon Ahx with two additional glycine units. Best results were obtained with c[Arg-GlyAsp-D-Phe-Lys(Biot-Ahx-Gly-Gly)-Gly-] with dissociation constants of K-D = 0.158 mu M from ELISA and K-D = 1.1 mu M 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. [References: 53]

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 Dates: 2000
 Publication Status: Published in print
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 Identifiers: eDoc: 318771
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Title: Biochemistry
  Alternative Title : Biochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 39 (40) Sequence Number: - Start / End Page: 12284 - 12294 Identifier: -