Electrochemical fabrication of reduced MoS-based portable molecular imprinting nanoprobe for selective SERS determination of theophylline.

A new portable molecular imprinting polymer (MIP)-SERS nanoprobe is fabricated by a convenient electrochemical method. Single-layered MoS is electrochemically reduced on a screen-printed electrode as the scaffold. Functional monomers o-phenylenediamine (oPD), template theophylline (THP), and SERS-active Au nanoparticles (AuNPs) are then one-step electropolymerized on the scaffold.

Development and characterization of a novel fusion protein of a mutated granulocyte colony-stimulating factor and human serum albumin in Pichia pastoris.

The purpose of the present work was to develop a novel, long-acting and potent human serum albumin/granulocyte colony stimulating factor (HSA/G-CSF) therapeutic fusion protein. The novel fusion protein, called HMG, was constructed by genetically fusing mutated human derived G-CSF (mG-CSF) to the C-terminal of HSA and then prepared in Pichia pastoris. The molecular mass of HMG was about 85 kDa and the isoelectric point was 5.

Engineering a pharmacologically superior form of granulocyte-colony-stimulating factor by fusion with gelatin-like-protein polymer.

The plasma half-life of therapeutic proteins is a critical factor in many clinical applications. Therefore, new strategies to prolong plasma half-life of long-acting peptides and protein drugs are in high demand. Here, we designed an artificial gelatin-like protein (GLK) and fused this hydrophilic GLK polymer to granulocyte-colony-stimulating factor (G-CSF) to generate a chimeric GLK/G-CSF fusion protein.

Preparation and characterization of a novel exendin-4 human serum albumin fusion protein expressed in Pichia pastoris.

A novel recombinant exendin-4 human serum albumin fusion protein (rEx-4/HSA) expressed in Pichia pastoris was prepared and characterized. Ex-4 is a 39-amino acid peptide isolated from the salivary gland of the lizard Heloderma suspectum and is thought to be a novel therapeutic agent for type 2 diabetes. But to gain a continued effect, the peptide has to be injected twice a day owing to its short plasma half-life (t(1/2) = 2.

[Pharmacokinetics of PEG-rhG-CSF and rHSA-hG-CSF in mice determined with ELISA].

Double antibody sandwich-type ELISA was used to detect rhG-CSF in serum to study the pharmacokinetics of rhG-CSF, PEG-rhG-CSF and rHSA-hG-CSF in mice and to confirm that PEGlyation and albumin fusion of rhG-CSF technology can prolong half-life of G-CSF. Pharmacokinetic parameters were calculated with 3P87 software. T1/2 s of rhG-CSF, PEG-rhG-CSF and rHSA-hG-CSF are 2.

Preparation and characterization of a potent, long-lasting recombinant human serum albumin-interferon-alpha2b fusion protein expressed in Pichia pastoris.

A long-lasting recombinant human serum albumin-interferon-alpha2b fusion protein (rHSA/IFNalpha2b) was prepared and its structure and biological activities were studied. rHSA/IFNalpha2b was expressed in methylotrophic yeast Pichia pastoris with HSA's natural signal peptide and purified by dye affinity chromatography, hydrophobic interaction chromatography, ion exchange chromatography and Sephadex G25. Purity of the prepared rHSA/IFNalpha2b was greater than 97% analyzed by non-reduced SDS-PAGE and RP-HPLC.