Forskning ved Københavns Universitet - Københavns Universitet

Forside

In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Standard

In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers. / Kaasgaard, T.; Ipsen, J. H.; Mouritsen, O. G.; Jørgensen, K.

I: Probe Microscopy, Bind 2, Nr. 2, 01.12.2001, s. 169-175.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Kaasgaard, T, Ipsen, JH, Mouritsen, OG & Jørgensen, K 2001, 'In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers', Probe Microscopy, bind 2, nr. 2, s. 169-175.

APA

Kaasgaard, T., Ipsen, J. H., Mouritsen, O. G., & Jørgensen, K. (2001). In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers. Probe Microscopy, 2(2), 169-175.

Vancouver

Kaasgaard T, Ipsen JH, Mouritsen OG, Jørgensen K. In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers. Probe Microscopy. 2001 dec 1;2(2):169-175.

Author

Kaasgaard, T. ; Ipsen, J. H. ; Mouritsen, O. G. ; Jørgensen, K. / In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers. I: Probe Microscopy. 2001 ; Bind 2, Nr. 2. s. 169-175.

Bibtex

@article{bf35bc91559f43d4b102f6ed5b7c5185,
title = "In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers",
abstract = "Atomic Force Microscopy (AFM) has been used to investigate the in situ phospholipase A2 (PLA2) degradation of one-component and two-component phospholipid mica supported bilayers composed of dipalmitoylphosphocholine (DPPC) and dimyristoylphosphocholine-distearoylphosphocholine (DMPC-DSPC). The solid supported phospholipid bilayers were imaged in contact mode AFM. Hydrolysis of the lipid bilayers was initiated by injection of PLA2 into the fluid cell of the atomic force microscope and the enzymatic degradation was monitored in situ at room temperature. The AFM pictures show that the PLA2 hydrolysis displays an increased activity towards certain preexisting interfacial regions in the one-component DPPC bilayer due to preformed holes appearing in the solid supported lipid film. It is found that the PLA2 hydrolysis activity, determined by the amount of lipid bilayer disappearing from the mica substrate, varies almost linearly as a function of time elapsed after addition of PLA2. For the equimolar DMPC-DSPC lipid bilayer mixture, an increased PLA2 activity is observed towards DMPC enriched small-scale lipid structures.",
keywords = "Atomic force microscopy, Interfaces, Langmuir Blodgett film, Lipid bilayer, Lipid domains, Phospholipase A, Phospholipids",
author = "T. Kaasgaard and Ipsen, {J. H.} and Mouritsen, {O. G.} and K. J{\o}rgensen",
year = "2001",
month = "12",
day = "1",
language = "English",
volume = "2",
pages = "169--175",
journal = "Probe Microscopy",
issn = "1355-185X",
publisher = "Taylor & Francis",
number = "2",

}

RIS

TY - JOUR

T1 - In situ atomic force microscope imaging of phospholipase A2 hydrolysis of one and two-component lipid bilayers

AU - Kaasgaard, T.

AU - Ipsen, J. H.

AU - Mouritsen, O. G.

AU - Jørgensen, K.

PY - 2001/12/1

Y1 - 2001/12/1

N2 - Atomic Force Microscopy (AFM) has been used to investigate the in situ phospholipase A2 (PLA2) degradation of one-component and two-component phospholipid mica supported bilayers composed of dipalmitoylphosphocholine (DPPC) and dimyristoylphosphocholine-distearoylphosphocholine (DMPC-DSPC). The solid supported phospholipid bilayers were imaged in contact mode AFM. Hydrolysis of the lipid bilayers was initiated by injection of PLA2 into the fluid cell of the atomic force microscope and the enzymatic degradation was monitored in situ at room temperature. The AFM pictures show that the PLA2 hydrolysis displays an increased activity towards certain preexisting interfacial regions in the one-component DPPC bilayer due to preformed holes appearing in the solid supported lipid film. It is found that the PLA2 hydrolysis activity, determined by the amount of lipid bilayer disappearing from the mica substrate, varies almost linearly as a function of time elapsed after addition of PLA2. For the equimolar DMPC-DSPC lipid bilayer mixture, an increased PLA2 activity is observed towards DMPC enriched small-scale lipid structures.

AB - Atomic Force Microscopy (AFM) has been used to investigate the in situ phospholipase A2 (PLA2) degradation of one-component and two-component phospholipid mica supported bilayers composed of dipalmitoylphosphocholine (DPPC) and dimyristoylphosphocholine-distearoylphosphocholine (DMPC-DSPC). The solid supported phospholipid bilayers were imaged in contact mode AFM. Hydrolysis of the lipid bilayers was initiated by injection of PLA2 into the fluid cell of the atomic force microscope and the enzymatic degradation was monitored in situ at room temperature. The AFM pictures show that the PLA2 hydrolysis displays an increased activity towards certain preexisting interfacial regions in the one-component DPPC bilayer due to preformed holes appearing in the solid supported lipid film. It is found that the PLA2 hydrolysis activity, determined by the amount of lipid bilayer disappearing from the mica substrate, varies almost linearly as a function of time elapsed after addition of PLA2. For the equimolar DMPC-DSPC lipid bilayer mixture, an increased PLA2 activity is observed towards DMPC enriched small-scale lipid structures.

KW - Atomic force microscopy

KW - Interfaces

KW - Langmuir Blodgett film

KW - Lipid bilayer

KW - Lipid domains

KW - Phospholipase A

KW - Phospholipids

UR - http://www.scopus.com/inward/record.url?scp=0035719359&partnerID=8YFLogxK

M3 - Journal article

AN - SCOPUS:0035719359

VL - 2

SP - 169

EP - 175

JO - Probe Microscopy

JF - Probe Microscopy

SN - 1355-185X

IS - 2

ER -

ID: 230987818