Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery

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Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery. / Jorgensen, Kent; Davidsen, Jesper; Mouritsen, Ole G.

In: FEBS letters, Vol. 531, No. 1, 30.10.2002, p. 23-27.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Jorgensen, K, Davidsen, J & Mouritsen, OG 2002, 'Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery', FEBS letters, vol. 531, no. 1, pp. 23-27. https://doi.org/10.1016/S0014-5793(02)03408-7

APA

Jorgensen, K., Davidsen, J., & Mouritsen, O. G. (2002). Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery. FEBS letters, 531(1), 23-27. https://doi.org/10.1016/S0014-5793(02)03408-7

Vancouver

Jorgensen K, Davidsen J, Mouritsen OG. Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery. FEBS letters. 2002 Oct 30;531(1):23-27. https://doi.org/10.1016/S0014-5793(02)03408-7

Author

Jorgensen, Kent ; Davidsen, Jesper ; Mouritsen, Ole G. / Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery. In: FEBS letters. 2002 ; Vol. 531, No. 1. pp. 23-27.

Bibtex

@article{833094b0b6954df5a711e4da61265874,
title = "Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery",
abstract = "Secretory phospholipase A2 (PLA2) is a ubiquitous water-soluble enzyme found in venom, pancreatic, and cancerous fluid. It is also known to play a role in membrane remodeling processes as well as in cellular signaling cascades. PLA2 is interfacially active and functions mainly on organized types of substrate, e.g. micelles and lipid bilayers. Hence the activity of the enzyme is modulated by the lateral organization and the physical properties of the substrate, in particular the structure in the nanometer range. The evidence for nano-scale structure and lipid domains in bilayers is briefly reviewed. Results obtained from a variety of experimental and theoretical studies of PLA2 activity on lipid-bilayer substrates are then presented which provide insight into the biophysical mechanisms of PLA2 activation on lipid bilayers and liposomes of different composition. The insight into these mechanisms has been used to propose a novel principle for liposomal drug targeting, release, and absorption triggered by secretory PLA2.",
keywords = "Anti-cancer drug, Lipid domain, Phospholipase A2, Pro-drug, Pro-enhancer, Stealth liposome",
author = "Kent Jorgensen and Jesper Davidsen and Mouritsen, {Ole G.}",
year = "2002",
month = "10",
day = "30",
doi = "10.1016/S0014-5793(02)03408-7",
language = "English",
volume = "531",
pages = "23--27",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "1",

}

RIS

TY - JOUR

T1 - Biophysical mechanisms of phospholipase A2 activation and their use in liposome-based drug delivery

AU - Jorgensen, Kent

AU - Davidsen, Jesper

AU - Mouritsen, Ole G.

PY - 2002/10/30

Y1 - 2002/10/30

N2 - Secretory phospholipase A2 (PLA2) is a ubiquitous water-soluble enzyme found in venom, pancreatic, and cancerous fluid. It is also known to play a role in membrane remodeling processes as well as in cellular signaling cascades. PLA2 is interfacially active and functions mainly on organized types of substrate, e.g. micelles and lipid bilayers. Hence the activity of the enzyme is modulated by the lateral organization and the physical properties of the substrate, in particular the structure in the nanometer range. The evidence for nano-scale structure and lipid domains in bilayers is briefly reviewed. Results obtained from a variety of experimental and theoretical studies of PLA2 activity on lipid-bilayer substrates are then presented which provide insight into the biophysical mechanisms of PLA2 activation on lipid bilayers and liposomes of different composition. The insight into these mechanisms has been used to propose a novel principle for liposomal drug targeting, release, and absorption triggered by secretory PLA2.

AB - Secretory phospholipase A2 (PLA2) is a ubiquitous water-soluble enzyme found in venom, pancreatic, and cancerous fluid. It is also known to play a role in membrane remodeling processes as well as in cellular signaling cascades. PLA2 is interfacially active and functions mainly on organized types of substrate, e.g. micelles and lipid bilayers. Hence the activity of the enzyme is modulated by the lateral organization and the physical properties of the substrate, in particular the structure in the nanometer range. The evidence for nano-scale structure and lipid domains in bilayers is briefly reviewed. Results obtained from a variety of experimental and theoretical studies of PLA2 activity on lipid-bilayer substrates are then presented which provide insight into the biophysical mechanisms of PLA2 activation on lipid bilayers and liposomes of different composition. The insight into these mechanisms has been used to propose a novel principle for liposomal drug targeting, release, and absorption triggered by secretory PLA2.

KW - Anti-cancer drug

KW - Lipid domain

KW - Phospholipase A2

KW - Pro-drug

KW - Pro-enhancer

KW - Stealth liposome

UR - http://www.scopus.com/inward/record.url?scp=0037201946&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(02)03408-7

DO - 10.1016/S0014-5793(02)03408-7

M3 - Journal article

C2 - 12401197

AN - SCOPUS:0037201946

VL - 531

SP - 23

EP - 27

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -

ID: 230986693