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

L. Khatri, K. M. G. Taylor, D. Q. M. Craig, K. Palin

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    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.
    Original languageEnglish
    Pages (from-to)113-118
    Number of pages6
    JournalInternational Journal of Pharmaceutics
    Volume322
    Issue number1-2
    DOIs
    Publication statusPublished - 2006

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