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Abstract
<p class="first" id="P1">In targeted drug delivery systems, it is desirable that the
delivery of hydrophobic
drugs to a cell or tissue is achieved with little to no side effects. To ensure that
the drugs do not leak during circulation, encapsulation stability of the drug carrier
in serum is critical. In this paper, we report on a modified FRET-based method to
evaluate encapsulation stability of amphiphilic assemblies and cross-linked 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.
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[1
]Department
of Chemistry, ‡Center for Bioactive Delivery, Institute for Applied
Life
Sciences, and §Molecular and Cellular Biology Program, University of Massachusetts,
Amherst, Massachusetts 01003, United States