Functionalization of biomaterials with small osteoinductive moieties

The aim of this study was to characterize the physicochemical properties of bacterial cellulose (BC) membranes functionalized with osteogenic growth peptide (OGP) and its C-terminal pentapeptide OGP[10–14], and to evaluate in vitro osteoinductive potential in early osteogenesis, besides, to evaluate cytotoxic, genotoxic and/or mutagenic effects. Peptide incorporation into the BC membranes did not change the morphology of BC nanofibers and BC crystallinity pattern. The characterization was complemented by Raman scattering, swelling ratio and mechanical tests. In vitro assays demonstrated no cytotoxic, genotoxic or mutagenic effects for any of the studied BC membranes. Culture with osteogenic cells revealed no difference in cell morphology among all the membranes tested. Cell viability/proliferation, total protein content, alkaline phosphatase activity and mineralization assays indicated that BC-OGP membranes enabled the highest development of the osteoblastic phenotype in vitro. In conclusion, the negative results of cytotoxicity, genotoxicity and mutagenicity indicated that all the membranes can be employed for medical supplies, mainly in bone tissue engineering/regeneration, due to their osteoinductive properties.

Characterization and in vitro evaluation of bacterial cellulose membranes functionalized with osteogenic growth peptide for bone tissue engineering

Oral vaccines: Design and delivery

This review is aimed at providing critical comments on selected approaches to formulating protein drugs into particulate forms feasible as practical pharmaceutical dosage forms. From a practical point of view, the need to formulate protein therapeutics into particulate forms includes inhalation and sustained-release delivery proteins, stabilizing and incorporating proteins into tissue engineering scaffolds and medical devices, as well as protecting and targeting protein therapeutics in an in vivo environment. For either of the applications, a common challenge is that proteins are easily denatured during particle-forming processes in which water–oil or water–air interfaces, multivalent ions or polyelectrolytes, strong shear stress and/or reactive crosslinking agents are often involved. Moreover, methods to protect proteins during the particle-forming processes must not compromise their pharmaceutical objectives, such as encapsulation efficiency, burst-free controlled release and storage convenience. Althou...

Formulating protein therapeutics into particulate forms.

Expression, purification, and characterization of recombinant human serum albumin fusion protein with two human glucagon-like peptide-1 mutants in Pichia pastoris.

Osteogenic growth peptide (OGP) was characterized in regenerating bone marrow, which can increase osteogenesis and hematopoiesis. The carboxy-terminal pentapeptide is a naturally occurring human and murine mitogen equipotent to OGP. In this study, we evaluated the potential role of OGP10-14 in regulation of hematopoiesis in human hematopoietic stem cells and animal model. Our results showed CD34+ stem cells from umbilical cord blood (UBC) were significantly increased in OGP10-14 treated samples, which is nearly equivalent to the results obtained from the combinations of IL3, IL11, G-CSF, and EPO group. OGP10-14 can also stimulate the differentiation of stem cells from bone marrow at the level of noncommitted progenitor stem cells, thus increasing the number of reconstituted red and white cells as well as platelets after injected i.m. everyday continuing for 5 days in hematopoietic function damage mice comparing with the OGP-untreated group. These data implicate that the role of OGP10-14 regulating hematopoiesis is in the early stage of the whole hematopoietic growth factors (HGFs) regulating network, just like the position of interleukin 13 in the hematopoiesis network.

C-terminal pentapeptide of osteogenic growth peptide regulates hematopoiesis in early stage.

The recombinant protein drug usually has a short half-life after intravenous (IV) or subcutaneous (SC) administration. The methods of prolonging the half-life of recombinant protein drug in common use are mainly based on three principles: 1 Amplifying the molecule weight of protein drug; 2 Making use of drug balance in the blood; 3 Reducing Immunogenicity. Three methods were focused on: Analog construction, PEGylation and Albumin fusion technology. The characteristics, half-life and immunogenicity problem of their products in the market and under development are summarized.

Advances in the Research of Long Life Recombinant Protein Drug

A recombinant plasmid pMM-CTB containing the gene for production of the nontoxic B subunit of Vibrio cholera was transferred into a safe, effective and attenuated oral vaccine Ty21a strain of Salmonella typhi. The resulting Ty21a (pMM-CTB) could steadily produce CT-B subunit that was secreted extracellularly and had the same antigenicity as CT-B produced by V. cholera. Furthermore, the characteristics of the antigenicity, the persistance in mice and the galactose sensitivity possessed in the strain of Ty21a were also retained in Ty21a (pMM-CTB). A bivalent vaccine containing Ty21a (pMM-CTB) and the killed whole cell of V. cholera was then constructed which had good immunogenecity for typhoid fever and cholera diarrhea.

Construction of a bivalent oral vaccine for prevention of typhoid fever and cholera diarrhea.

Cholera toxin B subunit (CTB) is considered to be an effective adjuvant and carrier protein. In order to make gene fusions, A plasmid pMC05 was constructed by introducing an unique EcoRI restriction endonuclease site at the 3^ end of CTB gene and the stop codon of CTB gene was removed at the same time so the fusion protein of CTB-beta-galactosidase alpha peptide could be expressed when pMC05 was transformed into E. coli, The abilities of the fusion protein to bind both ganglioside GM1 and CTB antibodies indicated that the fusion protein retains the bioligical function and the antigenicity of CTB. Our results show that gene fusions at the 3^ end of CTB provides a new approach for the construction of engineered peptide vaccines. Our studies also show that the transcriptional terminator sequence plays an important role in the high expression of the gene fusions. Based on the results, a vector-host system was established for the high expression of fusion proteins.

Construction of cholera toxin B subunit gene fusion system

The cloning in E. coli of a cholerae toxin gene that is A~-B~+ has been successfully constructed by using DNA recombinant techniques. E. coli cells carrying the recombinant plasmid pMM-CTB have been shown to produce a large amount of CTB subunits which are secreted as extracellular proteins.

THE EXPRESSION OF ENTEROTOXIN A - B + GENE OF V. cholerae IN E. coli

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