Naslov
The Effect of Heparin on Structural and Functional Properties of Low Density Lipoproteins

Autori
Kriško, Anita ; Piantanida, Ivo ; Kveder, Marina ; Pifat, Greta ; Lee, Anthony ; Greilberger, Joachim ; Kipmen-Korgun, Dijle ; Jürgens, Guenther

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Abstracts of the 4th COST D22 Workshop "Lipid-Protein Interactions" / - , 2005

Skup
COST D22 Workshop "Lipid-Protein Interactions" (4 ; 2005)

Mjesto i datum
Dubrovnik, Hrvatska, 06.10.2005. - 09.10.2005

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
LDL; heparin; fluorescence spectroscopy

Sažetak
Human plasma low density lipoproteins (LDLs) are supramolecular lipid-protein assemblies involved in the cholesterol transport in the bloodstream. They exhibit interesting structural complexity with the surface monolayer organization of phospholipids surrounding the hydrophobic core. Their structure is stabilized by apolipoprotein B100 (apoB), one of the largest monomeric proteins known with its 4536 aminoacid residues. Tertiary structure of the complex at atomic resolution has not yet been elucidated. Heparin is a linear polymer consisting of 1 4 linked pyranosyluronic acid and 2-amino-2-deoxyglucopyranose (glucosamine) residues. Apart from being abundant at the surface of artery walls, it is widely used as an anticoagulant drug. Therefore, its binding to LDL and its effect on the ability of LDL to bind to the LDL receptor have been investigated. Emphasis has been made on the physiological conditions of temperature, pH and the ionic strength. Intrinsic fluorescence spectroscopy of LDL has been applied to follow heparin binding. Fluorescence anisotropy has been measured to describe the changes in apoB and dansyl-heparin dynamics upon binding. Eu3+-labeled LDL binding to the intact LDL receptor has been monitored by time-resolved fluorescence spectroscopy technique. We have found that heparin binds to LDL under the physiological conditions, probably by Van der Waals interactions and hydrogen bonding. Temperature seems to be the most important factor influencing the interaction. Furthermore, the presence of heparin inhibits LDL binding to the intact LDL receptor that might have consequences on the cholesterol metabolism in vivo.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija

POVEZANOST RADA