Pregled bibliografske jedinice broj: 979583
Protonation of Long Chain Fatty Acids at the Membrane-Water Interface
Protonation of Long Chain Fatty Acids at the Membrane-Water Interface // Biophysical Journal, Volume 112, Issue 3, Supplement 1
San Francisco (CA), Sjedinjene Američke Države, 2017. str. p520a-p520a doi:10.1016/j.bpj.2016.11.2809 (poster, recenziran, sažetak, ostalo)
CROSBI ID: 979583 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Protonation of Long Chain Fatty Acids at the Membrane-Water Interface
Autori
Pashkovskaya, Alina A. ; Vazdar, Mario ; Jovanovic, Olga ; Pohl, Peter ; Pohl, Elena E.
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, ostalo
Izvornik
Biophysical Journal, Volume 112, Issue 3, Supplement 1
/ - , 2017, P520a-p520a
Skup
58th Annual Meeting of the Biophysical-Society
Mjesto i datum
San Francisco (CA), Sjedinjene Američke Države, 15.02.2014. - 19.02.2014
Vrsta sudjelovanja
Poster
Vrsta recenzije
Recenziran
Ključne riječi
fatty acid ; protonation ; bilayer ; molecular dynamics
Sažetak
Long-chain free fatty acids (FA) play an important role in several physiological and pathological processes such as lipid fusion, alteration of membrane permeability and fluidity, as well as regulation of enzyme and protein activity. FA-facilitated membrane proton transport (flip-flop) and FA-dependent proteinaceous proton transport (as in the case of mitochondrial uncoupling proteins) are governed by the difference between FA's pK and the pH in the immediate membrane vicinity1, 2. So far, a quantitative understanding of the process is hampered by the shift in the pK value of carboxylic groups that occurs upon moving the FA from the aqueous solutions into the membrane. Its molecular origin is not understood, conceivably because the reported pKa values for the same FA are scattered between 5 and 10.5. Here we systematically obtained the dependence of apparent pKa values on chain length, number and position of double bonds by measuring the zeta-potential of liposomes reconstituted with FA at different pH. pKa ranged from 6.4 to 7.6. Combining the zeta potential measurements with molecular dynamic simulations, we found that pK is determined by the interplay between the energetic costs for burying a charged moiety into the bilayer and the hydrophobic interactions between the free and lipid-bound fatty acid chains.
Izvorni jezik
Engleski
Znanstvena područja
Kemija
POVEZANOST RADA
Projekti:
HRZZ-UIP-2014-09-6090 - Molekularni aspekti oksidativnih procesa u stanicama (MolOxStress) (Vazdar, Mario, HRZZ - 2014-09) ( CroRIS)
Ustanove:
Institut "Ruđer Bošković", Zagreb
Profili:
Mario Vazdar
(autor)
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Conference Proceedings Citation Index - Science (CPCI-S)
- Scopus
- MEDLINE