For targeted drug delivery systems, delivery of hydrophobic drugs to a cell or tissue with small side effects is highly desired.  To ensure that the drugs do not leak during circulation, encapsulation stability of the drug carrier in serum is critical.  In this manuscript, we report on a modified FRET-based method to evaluate encapsulation stability of amphiphilic assemblies and crosslinked polymer assemblies in serum. Our results show that serum components can act as reservoirs for hydrophobic molecules.  We also show that serum albumin is likely to be the primary determinant of this property.  This work highlights the importance of assessing encapsulation stability in terms of dynamics of guest molecules, as it provides the critical distinction between hydrophobic molecules bound inside amphiphilic assemblies and the molecules that are bound to the hydrophobic pockets of serum albumin.<br/>

Importance of evaluating dynamic encapsulation stability of amphiphilic assemblies in serum

255th National Meeting (2018)

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