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Investigations of Lipid–Protein Interactions on Monolayers of Chain‐Substituted Phosphatidylcholines
Author(s) -
DahmenLevison Ursula,
Brezesinski Gerald,
Möhwald Helmuth,
Jakob Jens,
Nuhn Peter
Publication year - 2000
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20000804)39:15<2775::aid-anie2775>3.0.co;2-k
Subject(s) - monolayer , chemistry , phospholipase a2 , plasmalogen , hydrolysis , infrared spectroscopy , ether , vinyl ether , enzyme , lipase , phospholipid , stereochemistry , organic chemistry , biochemistry , copolymer , membrane , polymer
The interaction of phospholipase A 2 (PLA 2 ) and other interfacially active enzymes with lipids is strongly influenced by properties such as phase structure and de‐mixing phenomena. Lipid monolayers (see schematic representation) provide the opportunity to vary these properties in a systematic fashion and in combination with polarization‐modulated infrared reflection absorption spectroscopy (PM‐IRRAS) to quantify the enzyme activity. Chain‐substituted diester and plasmalogen‐analogous ether‐ester‐glycerophosphocholines were synthesized and their hydrolysis catalyzed by PLA 2 was investigated.