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Phospholipase A(2) hydrolysis of supported phospholipid bilayers: A neutron reflectivity and ellipsornetry study

Vacklin, H P; Tiberg, Fredrik LU ; Fragneto, G and Thomas, R K (2005) In Biochemistry 44(8). p.2811-2821
Abstract
We have investigated the phospholipase A(2) catalyzed hydrolysis of supported phospholipid bilayers using neutron reflection and ellipsometry. At the hydrophilic silica-water interface, hydrolysis of phosphatidy1choline bilayers by phospholipase A(2) from Naja mossambica mossambica venom is accompanied by destruction of the bilayer at an initial rate, which is comparable for DOPC and DPPC but is doubled for POPC. The extent of bilayer destruction at 25 degreesC decreases from DOPC to POPC and is dramatically reduced for DPPC. Neutron reflectivity measurements indicate that the enzyme penetrates into the bilayers in increasing order for DOPC, POPC, and DPPC, while the amount of enzyme adsorbed at the interface is smallest for DPPC and... (More)
We have investigated the phospholipase A(2) catalyzed hydrolysis of supported phospholipid bilayers using neutron reflection and ellipsometry. At the hydrophilic silica-water interface, hydrolysis of phosphatidy1choline bilayers by phospholipase A(2) from Naja mossambica mossambica venom is accompanied by destruction of the bilayer at an initial rate, which is comparable for DOPC and DPPC but is doubled for POPC. The extent of bilayer destruction at 25 degreesC decreases from DOPC to POPC and is dramatically reduced for DPPC. Neutron reflectivity measurements indicate that the enzyme penetrates into the bilayers in increasing order for DOPC, POPC, and DPPC, while the amount of enzyme adsorbed at the interface is smallest for DPPC and exhibits a maximum for POPC. Penetration into the hydrophobic chain region in the bilayer is further supported by the fact that the enzyme adsorbs strongly and irreversibly to a hydrophobic monolayer of octadecyltrichlorosilane. These results are rationalized in terms of the properties of the reaction products and the effect of their accumulation in the membrane on the kinetics of enzyme catalysis. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
44
issue
8
pages
2811 - 2821
publisher
The American Chemical Society
external identifiers
  • scopus:14344260441
ISSN
0006-2960
DOI
10.1021/bi047727a
language
English
LU publication?
yes
id
8e12b03b-6964-4237-994a-b4fea492801b (old id 157648)
date added to LUP
2007-07-12 13:33:17
date last changed
2017-07-30 03:38:08
@article{8e12b03b-6964-4237-994a-b4fea492801b,
  abstract     = {We have investigated the phospholipase A(2) catalyzed hydrolysis of supported phospholipid bilayers using neutron reflection and ellipsometry. At the hydrophilic silica-water interface, hydrolysis of phosphatidy1choline bilayers by phospholipase A(2) from Naja mossambica mossambica venom is accompanied by destruction of the bilayer at an initial rate, which is comparable for DOPC and DPPC but is doubled for POPC. The extent of bilayer destruction at 25 degreesC decreases from DOPC to POPC and is dramatically reduced for DPPC. Neutron reflectivity measurements indicate that the enzyme penetrates into the bilayers in increasing order for DOPC, POPC, and DPPC, while the amount of enzyme adsorbed at the interface is smallest for DPPC and exhibits a maximum for POPC. Penetration into the hydrophobic chain region in the bilayer is further supported by the fact that the enzyme adsorbs strongly and irreversibly to a hydrophobic monolayer of octadecyltrichlorosilane. These results are rationalized in terms of the properties of the reaction products and the effect of their accumulation in the membrane on the kinetics of enzyme catalysis.},
  author       = {Vacklin, H P and Tiberg, Fredrik and Fragneto, G and Thomas, R K},
  issn         = {0006-2960},
  language     = {eng},
  number       = {8},
  pages        = {2811--2821},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Phospholipase A(2) hydrolysis of supported phospholipid bilayers: A neutron reflectivity and ellipsornetry study},
  url          = {http://dx.doi.org/10.1021/bi047727a},
  volume       = {44},
  year         = {2005},
}