Phospholipids chiral at phosphorus: Synthesis of dioleoylthiophosphatidylcholine and stereospecificity of lecithin-cholesterol acyltransferase

Theresa Rosario-Jansen; Henry Pownal; Ru Tai Jiang; Ming Daw Tsai

doi:10.1016/0045-2068(90)90040-C

Phospholipids chiral at phosphorus: Synthesis of dioleoylthiophosphatidylcholine and stereospecificity of lecithin-cholesterol acyltransferase

Theresa Rosario-Jansen, Henry Pownal, Ru Tai Jiang, Ming Daw Tsai

Research output: Contribution to journal › Article

4 Scopus citations

Abstract

Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A₂, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable K_m and V_max values to R_p and S_p isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.

Original language	English (US)
Pages (from-to)	179-184
Number of pages	6
Journal	Bioorganic Chemistry
Volume	18
Issue number	2
DOIs	https://doi.org/10.1016/0045-2068(90)90040-C
State	Published - Jun 1990

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Drug Discovery
Organic Chemistry

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@article{a42cb659e0ea45ee98776082e94cef16,

title = "Phospholipids chiral at phosphorus: Synthesis of dioleoylthiophosphatidylcholine and stereospecificity of lecithin-cholesterol acyltransferase",

abstract = "Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A2, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable Km and Vmax values to Rp and Sp isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.",

author = "Theresa Rosario-Jansen and Henry Pownal and Jiang, {Ru Tai} and Tsai, {Ming Daw}",

year = "1990",

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language = "English (US)",

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pages = "179--184",

journal = "Bioorganic Chemistry",

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publisher = "Academic Press",

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T1 - Phospholipids chiral at phosphorus

T2 - Synthesis of dioleoylthiophosphatidylcholine and stereospecificity of lecithin-cholesterol acyltransferase

AU - Rosario-Jansen, Theresa

AU - Pownal, Henry

AU - Jiang, Ru Tai

AU - Tsai, Ming Daw

PY - 1990/6

Y1 - 1990/6

N2 - Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A2, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable Km and Vmax values to Rp and Sp isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.

AB - Chiral 1,2-dioleoyl-sn-glycero-3-thiophosphocholine (DOPsC) was synthesized from chiral 1,2-dipalmitoyl-sn-glycero-3-thiophosphocholine (DPPsC) via hydrolysis to sn-glycero-3-thiophosphatidylcholine followed by reacylation. Both DOPsC and DPPsC were used to probe the stereochemical requirement in the enzyme-substrate recognition of lecithincholesterol acyltransferase (LCAT) from human plasma. In contrast to phospholipase A2, LCAT is totally insensitive to sulfur substitution or configuration at phosphorus and gives indistinguishable Km and Vmax values to Rp and Sp isomers of DOPsC and DPPsC and the corresponding natural substrates. The results suggest lack of stereospecific interaction between LCAT and the phosphate group of phospholipids.

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