Thermodynamic and Kinetic Stability of DSPE-PEG(2000) Micelles in the Presence of Bovine Serum Albumin

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• 作者：Mark Kastantin ; Dimitris Missirlis ; Matthew Black ; Badriprasad Ananthanarayanan ; David Peters ; Matthew Tirrell
• 刊名：Journal of Physical Chemistry B
• 出版年：2010
• 出版时间：October 7, 2010
• 年：2010
• 卷：114
• 期：39
• 页码：12632-12640
• 全文大小：227K
• 年卷期：v.114,no.39(October 7, 2010)
• ISSN：1520-5207

文摘

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.