High sensitivity differential scanning calorimetry investigation of the interaction between liposomes, lactate dehydrogenase and tyrosinase

Khatri, L., Taylor, K. M. G., Craig, D. Q. M. and Palin, K. (2006) High sensitivity differential scanning calorimetry investigation of the interaction between liposomes, lactate dehydrogenase and tyrosinase. International Journal of Pharmaceutics, 322 (1-2). pp. 113-118. ISSN 0378-5173

Full text not available from this repository.

Abstract

High sensitivity differential scanning calorimetry (HSDSC) has been used to study the interaction of the model proteins lactate dehydrogenase (LDH) and tyrosinase with dimyristoylphosphatidylcholine (DMPC) liposomes, and relate this to the thermal and physical stability of the proteins. On beating, both LDH and tyrosinase denatured irreversibly in a time-dependent manner and modified the phase transition behaviour of DMPC liposomes at all concentrations investigated. The most marked effects occurred for the pretransition rather than the main phospholipid phase transition. The effects on the bilayer are likely to result from electrostatic interactions of the hydrophilic proteins with the head-groups of DMPC molecules, whilst due to their hydrophilic nature they do not penetrate into the bilayer. Tyrosinase is more highly ionised than LDH at the pH of the investigation, which may explain why tyrosinase has a greater effect than LDH on the HSDSC scans at mg/ml protein concentrations. (c) 2006 Elsevier B.V. All rights reserved.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Pharmacy
Depositing User:	Rachel Smith
Date Deposited:	16 May 2011 11:05
Last Modified:	24 Oct 2022 01:54
URI:	https://ueaeprints.uea.ac.uk/id/eprint/30488
DOI:	10.1016/j.ijpharm.2006.05.036

Actions (login required)

View Item