S-layer fusion protein as a tool functionalizing emulsomes and CurcuEmulsomes for antibody binding and targeting


Ucisik M. H., Küpcü S., Breitwieser A., Gelbmann N., Schuster B., Sleytr U. B.

Colloids and Surfaces B: Biointerfaces, cilt.128, ss.132-139, 2015 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 128
  • Basım Tarihi: 2015
  • Doi Numarası: 10.1016/j.colsurfb.2015.01.055
  • Dergi Adı: Colloids and Surfaces B: Biointerfaces
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.132-139
  • Anahtar Kelimeler: Emulsomes, Curcumin, S-layer (fusion) proteins, Immunoglobulin G (IgG) Targeting, Active drug delivery
  • İstanbul Medipol Üniversitesi Adresli: Hayır

Özet

Selective targeting of tumor cells by nanoparticle-based drug delivery systems is highly desirable because it maximizes the drug concentration at the desired target while simultaneously protecting the surrounding healthy tissues. Here, we show a design for smart nanocarriers based on a biomimetic approach that utilizes the building principle of virus envelope structures. Emulsomes and CurcuEmulsomes comprising a tripalmitin solid core surrounded by phospholipid layers are modified by S-layer proteins that self-assemble into a two-dimensional array to form a surface layer. One significant advantage of this nanoformulation is that it increases the solubility of the lipophilic anti-cancer agent curcumin in the CurcuEmulsomes by a factor of 2700. In order to make the emulsomes specific for IgG, the S-layer protein is fused with two protein G domains. This S-layer fusion protein preserves its recrystallization characteristics, forming an ordered surface layer (square lattice with 13. nm unit-by-unit distance). The GG domains are presented in a predicted orientation and exhibit a selective binding affinity for IgG.