Naslov
Do the myelin basic protein and phosphatidylcholine lipids like to dance together?

Autori
Maleš, Petra ; Brkljača, Zlatko ; Bakarić, Danijela

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

ISBN
978-953-6076-93-2

Skup
6. Simpozij studenata doktorskih studija PMF-a = 6th Faculty of Science PhD Student Symposium

Mjesto i datum
Zagreb, Hrvatska, 23.04.2022. - 24.04.2022

Vrsta sudjelovanja
Poster

Vrsta recenzije
Domaća recenzija

Ključne riječi
Phosphatidylcholine ; Liposomes ; MBP ; Lipids

Sažetak
Myelin is a multilayer membrane tightly wrapped around the axon of neurons, allowing efficient transmission of neural impulses. Slight changes in distributions of lipids in myelin membranes affect their adhesive properties, as well as their bonding with myelin basic protein (MBP), one of the most important myelin-associated proteins. With its high content of positively charged residues, unstructured MBP binds to the anionic lipids of the cytoplasmic leaflets, which causes balance changes between charged lipids and alternations in their lateral organization. All these changes appear in neurodegenerative diseases such as multiple sclerosis (MS) and encephalomyelitis (EAE). It is not yet known what role MBP confinement plays in the efficiency of its adsorption to lipid bilayer made from zwitterionic lipid 1, 2-dipalmitoyl-sn-glycero-3- phosphatidylcholine (DPPC), which constitutes about 40% of myelin lipids.Rather simple spectroscopic and calorimetric techniques such as FTIR spectroscopy, UV/Vis spectrophotometry and DSC can unravel the impact of MBP on phase transition temperatures (Tp, Tm) of DPPC multilamellar and unilamellar liposomes and their structural arrangements. Spectroscopic data will be analyzed with an appropriate chemometric tool.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA