Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 733-737 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 234 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 29 May 1997 |
| Externally published | Yes |
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Evidence for distinct behaviour of phosphatidylcholine and sphingomyelin at the low density lipoprotein surface. / Murphy, Helena C.; Ala-Korpela, Mika; White, John J.; Raoof, Alia; Bell, Jimmy D.; Barnard, Maria L.; Burns, Shamus P.; Iles, Richard A.
In: Biochemical and Biophysical Research Communications, Vol. 234, No. 3, 29.05.1997, p. 733-737.Research output: Contribution to journal › Article
TY - JOUR
T1 - Evidence for distinct behaviour of phosphatidylcholine and sphingomyelin at the low density lipoprotein surface
AU - Murphy, Helena C.
AU - Ala-Korpela, Mika
AU - White, John J.
AU - Raoof, Alia
AU - Bell, Jimmy D.
AU - Barnard, Maria L.
AU - Burns, Shamus P.
AU - Iles, Richard A.
PY - 1997/5/29
Y1 - 1997/5/29
N2 - This study demonstrates that the use of high field 1H NMR spectroscopy permits individual detection of phosphatidylcholine and sphingomyelin molecules at the surface of native low density lipoprotein (LDL) particles. Distinct behaviour was observed for the choline head group -N(CH3)3 resonances of these different phospholipids revealing preferential immobilisation for phosphatidylcholine. This suggests the existence of reversible and irreversible phosphatidylcholine-apolipoprotein B interactions and is consistent with microdomain formation at the surface monolayer of LDL. The novel resonance assignment and results show that 1H NMR can provide efficient and practical means for future studies on the structure and dynamics at the LDL surface.
AB - This study demonstrates that the use of high field 1H NMR spectroscopy permits individual detection of phosphatidylcholine and sphingomyelin molecules at the surface of native low density lipoprotein (LDL) particles. Distinct behaviour was observed for the choline head group -N(CH3)3 resonances of these different phospholipids revealing preferential immobilisation for phosphatidylcholine. This suggests the existence of reversible and irreversible phosphatidylcholine-apolipoprotein B interactions and is consistent with microdomain formation at the surface monolayer of LDL. The novel resonance assignment and results show that 1H NMR can provide efficient and practical means for future studies on the structure and dynamics at the LDL surface.
UR - http://www.scopus.com/inward/record.url?scp=18344402604&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1997.6634
DO - 10.1006/bbrc.1997.6634
M3 - Article
C2 - 9175784
AN - SCOPUS:18344402604
VL - 234
SP - 733
EP - 737
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -