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Interaction kinetics of serum proteins with liposomes and their effect on phospholipase-induced liposomal drug release.

Authors :
Shibata H
Yoshida H
Izutsu K
Haishima Y
Kawanishi T
Okuda H
Goda Y
Source :
International journal of pharmaceutics [Int J Pharm] 2015 Nov 30; Vol. 495 (2), pp. 827-39. Date of Electronic Publication: 2015 Sep 26.
Publication Year :
2015

Abstract

We used surface plasmon resonance (SPR) to measure the affinity and kinetics of the interaction between serum proteins and both conventional and PEGylated liposomes. The effect of the interactions on secretory phospholipase A2 (sPLA2)-induced release of a model drug from liposomes was also assessed. SPR analysis of 12 serum proteins revealed that the mode of interaction between serum proteins and liposomes greatly varies depending on the type of protein. For example, albumin bound to liposomes at slower association/dissociation rates with higher affinity and prevented sPLA2-induced drug release from PEGylated liposomes. Conversely, fibronectin bound at faster association/dissociation rates with lower affinity and demonstrated little impact on the drug release. These results indicate that the effect of serum proteins on sPLA2 phospholipid hydrolysis varies with the mode of interaction between proteins and liposomes. Understanding how the proteins interact with liposomes and impact sPLA2 phospholipid hydrolysis should aid the rational design of therapeutic liposomal formulations.<br /> (Copyright © 2015 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-3476
Volume :
495
Issue :
2
Database :
MEDLINE
Journal :
International journal of pharmaceutics
Publication Type :
Academic Journal
Accession number :
26410758
Full Text :
https://doi.org/10.1016/j.ijpharm.2015.09.053