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Projects / Programmes source: ARIS

Molecular recognition in biological systems'

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Periods
January 1, 1999 - December 31, 2003
Research activity

Code Science Field Subfield
1.05.00  Natural sciences and mathematics  Biochemistry and molecular biology   
1.09.00  Natural sciences and mathematics  Pharmacy   

Code Science Field
P003  Natural sciences and mathematics  Chemistry 
P004  Natural sciences and mathematics  Biochemistry, Metabolism 
B002  Biomedical sciences  Biophysics 
B007  Biomedical sciences  Medicine (human and vertebrates) 
Evaluation (rules)
source: COBISS
Evaluation of bibliographic research performance indicators according to ARIS methodology
Citations Citations for bibliographic records in COBIB.SI that are linked to records in citation databases
source: WoS source: Scopus source: COBISS
Researchers (6)
no. Code Name and surname Research area Role Period No. of publications
1.  06628  PhD Roman Jerala  Biochemistry and molecular biology  Researcher  2001 - 2003  0 
2.  02566  PhD Jurkica Kidrič  Pharmacy  Head  2001 - 2003  0 
3.  17916  PhD Iztok Jože Košir  Chemistry  Researcher  2001 - 2002  0 
4.  17917  PhD Andreja Majerle  Biotechnology  Researcher  2001 - 2002  0 
5.  21426  PhD Mateja Manček Keber  Pharmacy  Researcher  2001 - 2003  0 
6.  12060  PhD Primož Pristovšek  Chemistry  Researcher  2001 - 2003  0 
Organisations (1)
no. Code Research organisation City Registration number No. of publications
1.  0104  National Institute of Chemistry  Ljubljana  5051592000  10 
Abstract
We have prepared recombinant CD14 and a CD14 fragment consisting of its first 152 residues. This is the first report of the expression of CD14 in a yeast or bacterial system. Both rCD14s were able to bind lipopolysaccharides (LPS). On the basis of CD and fluorescence spectra taking into account that CD14 contains 10 leucine-rech repeats we hypothesize that CD14 contains a mixture of ?- and ?-type structures. We proposed the model for complex between LPS or its active moiety lipid A and polymyxins B and E (peptides neutralizing LPS toxicity) on the basis of NMR and molecular modeling studies. Proposed binding mode breaks the supramolecular structure of LPS connected with its toxicity. The model should contribute to the understanding of entropy-driven PmB-lipid A binding at the molecular level and assist the design of inhibotors of endotoxic activity. Using biophysical (UV, CD, NMR) and biochemical methods we have demonstrated that stefin A forms dimers under denaturating conditions. The dimer is a folded and structured protein although it no more inhibits cysteine proteases. The formation of stefin dimers might, besides representing a model for conformational transitions in dimerization of small single domain proteins, also have physiological relevance for the regulation of its ability to inhibit proteases and for its incorporation into polymerized cell envelope.
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