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Nanoerythrosomes tailoring: Lipid induced protein scaffolding in ghost membrane derived vesicles

  • Róbert Deák
  • , Judith Mihály
  • , Imola Cs Szigyártó
  • , Tamás Beke-Somfai
  • , Lilla Turiák
  • , László Drahos
  • , András Wacha
  • , Attila Bóta
  • , Zoltán Varga

Research output: Contribution to journalArticlepeer-review

Abstract

A peculiar polygonal protein scaffolding that resembles to spectrin-based skeleton of red blood cells can be reconstructed on the outer surface of vesicle-like nanoerythrosomes. The approximately 130 nm sized nanoerythrosomes are produced from red blood cell ghosts by addition of phospholipids (dipalmitoylphosphatidylcholine, DPPC). The scaffolding, constructed from the structural proteins of the cell membrane skeleton, covers the whole object resulting an enhanced stiffness. The protein pattern of the scaffolding is thermosensitive, reversible transformable in the biologically relevant temperature range. When the lipid additive is changed from DPPC to lysophospholipid (LPC), the protein network/scaffolding ceases to exist. By the variation of lipid type and ratio, a tailoring of the nanoerythrosomes can be achieved. During the tailoring process nanoerythrosomes or micelles, in a wide size range from 200 to 30 nm, are produced.

Original languageEnglish (US)
Article number110428
JournalMaterials Science and Engineering C
Volume109
DOIs
StatePublished - Apr 2020
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by the National Research Development and Innovation Office (Hungary) under grant numbers PD 121326 and NVKP_16-1-2016-0007 , HunProtExc (A. Bóta) and Protein research program of Hungarian Academy of Sciences (MEDinPROT, A. Bóta). Z. Varga was supported by the János Bolyai Research Fellowship of the Hungarian Academy of Sciences . We thank Teréz Kiss for freeze fracturing and Ferenc Zsila for reviewing polarized light spectroscopy measurements.

Publisher Copyright:
© 2019

Keywords

  • Ghost
  • Nanoerythrosome
  • Protein - lipid interactions
  • Protein network
  • Protein scaffolding

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