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

Ucisik, Mehmet Hikmet; Küpcü, Seta; Breitwieser, Andreas; Gelbmann, Nicola; Schuster, Bernhard; Sleytr, Uwe B.

doi:10.1016/j.colsurfb.2015.01.055

Cited by 30 publications

(32 citation statements)

References 46 publications

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“…The recombinant S-layer protein was over-expressed in E. coli and accumulated in inclusion body like structures, which were stored after a downstream processing including a homogenization step at −20 °C [26,46]. Subsequently, the protein was extracted with 5 M guanidine hydrochloride (GHCL, Gerbu Nr.…”

Section: Methodsmentioning

confidence: 99%

In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers

Breitwieser

Iturri

Toca-Herrera

et al. 2017

IJMS

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The recombinant bacterial surface layer (S-layer) protein rSbpA of Lysinibacillus sphaericus CCM 2177 is an ideal model system to study non-classical nucleation and growth of protein crystals at surfaces since the recrystallization process may be separated into two distinct steps: (i) adsorption of S-layer protein monomers on silicon surfaces is completed within 5 min and the amount of bound S-layer protein sufficient for the subsequent formation of a closed crystalline monolayer; (ii) the recrystallization process is triggered—after washing away the unbound S-layer protein—by the addition of a CaCl2 containing buffer solution, and completed after approximately 2 h. The entire self-assembly process including the formation of amorphous clusters, the subsequent transformation into crystalline monomolecular arrays, and finally crystal growth into extended lattices was investigated by quartz crystal microbalance with dissipation (QCM-D) and atomic force microscopy (AFM). Moreover, contact angle measurements showed that the surface properties of S-layers change from hydrophilic to hydrophobic as the crystallization proceeds. This two-step approach is new in basic and application driven S-layer research and, most likely, will have advantages for functionalizing surfaces (e.g., by spray-coating) with tailor-made biological sensing layers.

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Section: Methodsmentioning

confidence: 99%

In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers

Breitwieser

Iturri

Toca-Herrera

et al. 2017

IJMS

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“…111 Furthermore, emulsomes, a liposome-like supramolecular nanostructure, could be modified by IgG with the help of Slp. Ücisik et al 137 developed rSbpA-GG-coated Curcuemulsomes (Figure 9B), in which rSbpA-GG was an Slfp containing SbpA and two protein G domains (IgG-binding domains). ELISAs verified that the fusion of protein G domains with SbpA preserved their IgG-binding feature.…”

Section: Immobilization Of Biomacromoleculesmentioning

confidence: 99%

“…In 2015, Ücisik et al published a research paper reporting that Slp coating as a matrix helped the emulsome-entrapped antitumor drug curcumin (Curcuemulsome) to immobilize and target human antibody IgG. 137 This study involved protein fusion technology. Two protein G domains possessing specific IgG affinity were fused with SbpA.…”

Section: Drug Deliverymentioning

confidence: 99%

“…However, Ücisik et al unfortunately did not further evaluate the in vivo targeted drug delivery efficiency or the cancer therapeutic efficiency of rSbpA-GG-coated Curcuemulsomes. 137 As we continue to explore design strategies, our progress in oral delivery of biomacromolecular drugs and targeted drug delivery by Slp-coated liposomes will continue. We also believe that the biomedical engineering uses of Slp combined with the favorable characteristics of liposomes will drive a series of biomedical applications.…”

Section: Drug Deliverymentioning

confidence: 99%

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<p>Slp-coated liposomes for drug delivery and biomedical applications: potential and challenges</p>

Luo¹,

Yang²,

Yao³

et al. 2019

IJN

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Slp forms a crystalline array of proteins on the outermost envelope of bacteria and archaea with a molecular weight of 40-200 kDa. Slp can self-assemble on the surface of liposomes in a proper environment via electrostatic interactions, which could be employed to functionalize liposomes by forming Slp-coated liposomes for various applications. Among the molecular characteristics, the stability, adhesion, and immobilization of biomacromolecules are regarded as the most meaningful. Compared to plain liposomes, Slp-coated liposomes show excellent physicochemical and biological stabilities. Recently, Slp-coated liposomes were shown to specifically adhere to the gastrointestinal tract, which was attributed to the "ligand-receptor interaction" effect. Furthermore, Slp as a "bridge" can immobilize functional biomacromolecules on the surface of liposomes via protein fusion technology or intermolecular forces, endowing liposomes with beneficial functions. In view of these favorable features, Slp-coated liposomes are highly likely to be an ideal platform for drug delivery and biomedical uses. This review aims to provide a general framework for the structure and characteristics of Slp and the interactions between Slp and liposomes, to highlight the unique properties and drug delivery as well as the biomedical applications of the Slp-coated liposomes, and to discuss the ongoing challenges and perspectives.

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“…As a matter of fact, functional groups on the protein lattice are arranged in well-defined positions and orientations [22,24]. Examples are affinity matrices with S-layer fusion proteins carrying the immunoglobulin G (IgG) binding domains of Protein A or Protein G [29][30][31] or the green fluorescent protein (GFP and its variants) for Förster-or Fluorescence-energy transfer (FRET) pairs in DNA-hairpin sensors [32]. In this context, it has to be stressed that the high binding capacity of S-layer proteins would also be retained after intra-and intermolecular crosslinking (e.g., by glutardialdehyde or Dimethyl-pimelimidatedihydrochloride (DMP)).…”

Section: Introductionmentioning

confidence: 99%

S-Layer Protein Coated Carbon Nanotubes

et al. 2019

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Carbon nanotubes (CNTs) have already been considered for medical applications due to their small diameter and ability to penetrate cells and tissues. However, since CNTs are chemically inert and non-dispersible in water, they have to be chemically functionalized or coated with biomolecules to carry payloads or interact with the environment. Proteins, although often only randomly bound to the CNT surface, are preferred because they provide a better biocompatibility and present functional groups for binding additional molecules. A new approach to functionalize CNTs with a closed and precisely ordered protein layer is offered by bacterial surface layer (S-layer) proteins, which have already attracted much attention in the functionalization of surfaces. We could demonstrate that bacterial S-layer proteins (SbpA of Lysinibacillus sphaericus CCM 2177 and the recombinant fusion protein rSbpA31-1068GG comprising the S-layer protein and two copies of the IgG binding region of Protein G) can be used to disperse and functionalize oxidized multi walled CNTs. Following a simple protocol, a complete surface coverage with a long-range crystalline S-layer lattice can be obtained. When rSbpA31-1068GG was used for coating, the introduced functionality could be confirmed by binding gold labeled antibodies via the IgG binding domain of the fusion protein. Since a great variety of functional S-layer fusion proteins has already been described, our new technology has the potential for a broad spectrum of functionalized CNTs.

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

Abstract: Graphical abstract

Cited by 30 publications

References 46 publications

In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers

In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers

<p>Slp-coated liposomes for drug delivery and biomedical applications: potential and challenges</p>

S-Layer Protein Coated Carbon Nanotubes

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