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Projects / Programmes source: ARIS

Structural-based neutralization of endotoxin by peptides

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Research activity

Code Science Field Subfield
1.09.00  Natural sciences and mathematics  Pharmacy   

Code Science Field
B470  Biomedical sciences  Physiology 
Keywords
LPS; immune response, peptidic inhibitors of LPS; molecular recognition; rational drug design
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 (8)
no. Code Name and surname Research area Role Period No. of publications
1.  18675  Robert Bremšak    Technical associate  2004 - 2007  11 
2.  17915  PhD Helena Gradišar  Biotechnology  Researcher  2004 - 2006  130 
3.  23940  PhD Boštjan Japelj  Physics  Junior researcher  2004 - 2007  38 
4.  06628  PhD Roman Jerala  Biochemistry and molecular biology  Researcher  2004 - 2007  1,189 
5.  17917  PhD Andreja Majerle  Biotechnology  Researcher  2004 - 2007  92 
6.  12048  PhD Marjetka Podobnik  Biochemistry and molecular biology  Researcher  2007  316 
7.  12060  PhD Primož Pristovšek  Chemistry  Head  2004 - 2007  135 
8.  22575  PhD Primož Šket  Chemistry  Researcher  2007  217 
Organisations (1)
no. Code Research organisation City Registration number No. of publications
1.  0104  National Institute of Chemistry  Ljubljana  5051592000  20,942 
Abstract
Lipopolysaccharide (LPS) triggers a series of defense reaction in the body that may lead to septic shock which is a leading cause of death in intensive care units and according to estimates, causes in the European union more than 150.000 casualties annually. One of the important strategies of preventing sepsis is aimed at its neutralization by specific binding of peptides that are derived from natural defense proteins or peptides. In continuation of our previous work where we have determined the bound tertiary structures of a series of peptides we will study additional structural aspects of LPS binding to peptidic inhibitors. We will determine the peptide stuctures when bound to LPS using NMR techniques while we approach the structures of the complex using computer modeling. We plan to refine the pharmacophore - the common LPS binding motif that we have already extended in our previous work by evaluating besides electrostatic also hydrophobic interactions. The course of action will include repeated cycles of designing new peptides with altered properties, their synthesis, structure analysis and determination of their characteristics, e.g. binding of LPS (Kd), neutralization of cell activation by LPS and any toxicity towards human cells. All the necessary equipment and knowledge for the execution of such a complex task is available in the research group. We expect that the project will provide the basis for rational design of novel peptide inhibitors of LPS activity.
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