Structural-based neutralization of endotoxin by peptides

Code

J1-6357 (C) - included in ARRS records

Head

PhD Primož Pristovšek

Period

7/1/2004 - 6/30/2007

Range in 2007

0.29 FTE

Science

Natural sciences and mathematics (5)
Biotechnical sciences (2)
Other (1)

Reseacher status

Researcher (7)
Junior expert or technical associate (1)
Junior researcher (0)
Researcher/expert (0)
Private researcher (0)

Education

Doctor's degree (7)
Other (1)

Sex

Woman (3)
Man (5)

Status

Active (8)

No. of publications

10–99 (3)
100–999 (4)
1,000–9,999 (1)

Projects / Programmes source: ARRS

source: ARRS

Structural-based neutralization of endotoxin by peptides

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

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 publicationsNo. of publications
1.	18675	Robert Bremšak		Technician	2004 - 2007	11
2.	17915	PhD Helena Gradišar	Biotechnical sciences	Researcher	2004 - 2006	125
3.	23940	PhD Boštjan Japelj	Natural sciences and mathematics	Junior researcher	2004 - 2007	37
4.	06628	PhD Roman Jerala	Natural sciences and mathematics	Researcher	2004 - 2007	1,141
5.	17917	PhD Andreja Majerle	Biotechnical sciences	Researcher	2004 - 2007	92
6.	12048	PhD Marjetka Podobnik	Natural sciences and mathematics	Researcher	2007	291
7.	12060	PhD Primož Pristovšek	Natural sciences and mathematics	Principal Researcher	2004 - 2007	135
8.	22575	PhD Primož Šket	Natural sciences and mathematics	Researcher	2007	211

Organisations (1)

no.	Code	Research organisation	City	Registration number	No. of publicationsNo. of publications
1.	0104	National Institute of Chemistry	Ljubljana	5051592000	21,093

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.