Thermodynamic and kinetic stability of DSPE-PEG(2000) micelles in the presence of bovine serum albumin

Mark Kastantin, Dimitris Missirlis, Matthew Black, Badriprasad Ananthanarayanan, David Peters, Matthew Tirrell

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

This work investigated the stability of DSPE-PEG(2000) micelles in the presence of bovine serum albumin (BSA). DSPE-PEG(2000) was found to exist in equilibrium among monomeric, micellar, and BSA-bound states, and this equilibrium shifted toward the BSA-bound state when the temperature increased from 20 to 37°C. The micellar state is thermodynamically unstable at both temperatures when the concentration of BSA approaches that of DSPE-PEG(2000), and micelle breakup occurs with a first-order time constant of 130±9 min at 20°C and 7.8±1.6 min at 37°C. Thus, previous targeting experiments that demonstrate synergistic effects in multiply functionalized DSPE-PEG(2000) micelles are likely due to targeting that occurs on a timescale faster than that of micelle breakup. Micelle breakup was limited by diffusion at 20°C whereas at 37°C monomer desorption from the micelle was the rate-limiting step. These findings give clear guidance concerning the lifetimes of micelles that may be used as diagnostic and therapeutic nanoparticles.

Original languageEnglish (US)
Pages (from-to)12632-12640
Number of pages9
JournalJournal of Physical Chemistry B
Volume114
Issue number39
DOIs
StatePublished - Oct 7 2010
Externally publishedYes

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