dc.contributor.author | Üçışık, Mehmet | |
dc.contributor.author | Küpçü, Seda | |
dc.contributor.author | Breitwieser, Andreas | |
dc.contributor.author | Gelbmann, Nicola | |
dc.contributor.author | Schuster, Bernhard | |
dc.contributor.author | Sleytr, Uwe | |
dc.date.accessioned | 10.07.201910:49:13 | |
dc.date.accessioned | 2019-07-10T19:51:30Z | |
dc.date.available | 10.07.201910:49:13 | |
dc.date.available | 2019-07-10T19:51:30Z | |
dc.date.issued | 2015 | en_US |
dc.identifier.citation | Üçışık, M. H., Küpçü, S., Breitwieser, A., Gelbmann, N., Schuster, B. ve Sleytr, U. B. (2015). S-layer fusion protein as a tool functionalizing emulsomes and CurcuEmulsomes for antibody binding and targeting. Colloids and Surfaces B: Biointerfaces, 128, 132-139. https://dx.doi.org/10.1016/j.colsurfb.2015.01.055 | en_US |
dc.identifier.issn | 0927-7765 | |
dc.identifier.issn | 1873-4367 | |
dc.identifier.uri | https://dx.doi.org/10.1016/j.colsurfb.2015.01.055 | |
dc.identifier.uri | https://hdl.handle.net/20.500.12511/2229 | |
dc.description | WOS: 000353930000019 | en_US |
dc.description | PubMed ID: 25734967 | en_US |
dc.description.abstract | 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. | en_US |
dc.description.sponsorship | US Air Force Office of Scientific Research (AFOSR) [FA9550-09-0342, FA9550-10-1-0223]; Austrian Science Fund (FWF) [P-20256-B11] | en_US |
dc.description.sponsorship | The work was supported by US Air Force Office of Scientific Research (AFOSR), Agreement Award Nr.: FA9550-09-0342 and Agreement Award Nr.: FA9550-10-1-0223, and the Austrian Science Fund (FWF), project P-20256-B11. The authors thank Marcin Laskiewicz and Jaqueline Friedmann for their assistance in AFM experiments. The authors also thank to Dr. Monika Debreczeny for the confocal laser scanning microscopy analysis carried out at the Imaging Center of the Vienna Institute of BioTechnology (VIBT). | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | info:eu-repo/semantics/openAccess | en_US |
dc.rights | Attribution 4.0 International | * |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | Emulsomes | en_US |
dc.subject | Curcumin | en_US |
dc.subject | S-layer (fusion) Proteins | en_US |
dc.subject | Immunoglobulin G (IgG) Targeting | en_US |
dc.subject | Active Drug Delivery | en_US |
dc.title | S-layer fusion protein as a tool functionalizing emulsomes and CurcuEmulsomes for antibody binding and targeting | en_US |
dc.type | article | en_US |
dc.relation.ispartof | Colloids and Surfaces B: Biointerfaces | en_US |
dc.department | İstanbul Medipol Üniversitesi, Mühendislik ve Doğa Bilimleri Fakültesi, Biyomedikal Mühendisliği Bölümü | en_US |
dc.authorid | 0000-0001-9434-3861 | en_US |
dc.identifier.volume | 128 | en_US |
dc.identifier.startpage | 132 | en_US |
dc.identifier.endpage | 139 | en_US |
dc.relation.publicationcategory | Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı | en_US |
dc.identifier.doi | 10.1016/j.colsurfb.2015.01.055 | en_US |
dc.identifier.wosquality | Q1 | en_US |
dc.identifier.scopusquality | Q1 | en_US |