Projects / Programmes source: ARIS

Micro and nano particles in biotechnology

Research activity

Code Science Field Subfield
4.06.00  Biotechnical sciences  Biotechnology   

Code Science Field
T000  Technological sciences   
recombinant proteins; biopharmaceuticals; micro-particles; nano-particles; biolistic transformation; Escherichia coli; Pichia pastoris; TNF-alpha, GFP; inclusion bodies; micro-aggregation; macromolecular aggregates; histidine tags;
Evaluation (rules)
source: COBISS
Researchers (9)
no. Code Name and surname Research area Role Period No. of publicationsNo. of publications
1.  20381  PhD Irena Fonda  Biochemistry and molecular biology  Researcher  2004 - 2007  43 
2.  06108  PhD Vladimira Gaberc-Porekar  Biotechnology  Researcher  2004 - 2007  220 
3.  26055  PhD Gorazd Hribar  Biochemistry and molecular biology  Junior researcher  2005 - 2007  49 
4.  17276  Jelka Lenarčič    Technical associate  2004 - 2005 
5.  21241  PhD Ana Lenassi Zupan  Biotechnology  Researcher  2004  16 
6.  01494  PhD Viktor Menart  Biotechnology  Head  2004 - 2007  162 
7.  23123  MSc Tatjana Milunović  Biotechnology  Researcher  2004 - 2007  28 
8.  22580  PhD Špela Peternel  Biochemistry and molecular biology  Junior researcher  2004 - 2007  42 
9.  12060  PhD Primož Pristovšek  Chemistry  Researcher  2004 - 2007  135 
Organisations (1)
no. Code Research organisation City Registration number No. of publicationsNo. of publications
1.  0104  National Institute of Chemistry  Ljubljana  5051592000  21,377 
Research project "Micro and Nano Particles in Biotechnology" is composed of two segments that play a central role in development of modern bio-pharmaceuticals. Common to both parts are knowledge and technology development for preparation and characterization of protein micro and nano particles applicable in modern biotechnology. The first part involves intracellular micro-aggregation of proteins leading to inclusion body formation. According to our hypothesis (already partially confirmed) that in some properly folded proteins (e.g. TNF-alpha) micro-aggregation and inclusion body formation can be controlled by modulation of hydrophobicity/hydrophylicity of the affinity oligo-histidine tag. We propose a novel function and applicability of histidine tags, primarily used for easier protein isolation. During biosynthesis inclusion bodies will serve for protein storage with the aim of directing and controlling micro-aggregation and precipitation of biologically active proteins, but not improperly folded ones. TNF-alpha will be the main oligomeric protein model and GFP a monomeric, both with histidine tags attached to the N-termini. Design of novel "hybrid" histidine tags for above described purposes is also anticipated. The second part deals with preparation of macro-molecular aggregates (nano particles) of highly purified recombinant proteins as a new approach to pharmaceutical formulations. An original way of using controlled and reversible micro-aggregation of histidine-tagged molecules upon metal ion addition will be applied. This should further result in development of protein formulations with sustained release and higher in vivo stability.
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