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Car☐yacyl derivatives of cardiolipin as four-tailed hydrophobic anchors for the covalent coupling of hydrophilic proteins to liposomes

Authors
Journal
Biochimica et Biophysica Acta (BBA) - Biomembranes
0005-2736
Publisher
Elsevier
Publication Date
Volume
1070
Issue
2
Identifiers
DOI: 10.1016/0005-2736(91)90080-r
Keywords
  • Car☐Yacyl Derivative
  • Cardiolipin
  • Liposome
  • Proteoliposome
  • Covalent Coupling
  • Chymotrypsin
  • Antibody
Disciplines
  • Biology

Abstract

Abstract Two car☐yacyl derivatives of cardiolipin, O-succinyl- and O-glutarylcardiolipin, were synthesized with the aim of using them as artificial membrane anchors for the immobilization of hydrophilic proteins to liposomes. Four adjacent fatty acid residues can be introduced into a protein with only one single amino group being blocked, by reacting the cardiolipin derivatives with the protein amino groups after carbodiimide activation. α-Chymotrypsin, used as a model protein, and modified with on average two molecules of O-succinylcardiolipin was incorporated into liposomes, which had been prepared by different methods, with very high yield. If incorporated in performed liposomes, the car☐yacyl cardiolipin anchors were also efficient in binding proteins to liposomal surfaces. Up to 350 μg chymotrypsin / μ mol lipid were coupled to small unilamellar vesicles, preserving reactivity of the enzyme towards specific macromolecular inhibitors. Human IgG could also be bound to anchor-containing liposomes with high protein to lipid coupling ratio as well as high coupling yield.

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