(391c) Encapsulating Proteins into Complex Coacervates
AIChE Annual Meeting
2019
2019 AIChE Annual Meeting
Materials Engineering and Sciences Division
Biomaterials for Immunological Applications
Tuesday, November 12, 2019 - 4:06pm to 4:24pm
Sarah Perry Sarah Perry 2 0 2019-04-11T19:15:00Z 2019-04-11T19:15:00Z 1 256 1465 University of Massachusetts Amherst 12 3 1718 14.0
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mso-bidi-font-family:" times new roman>80% of the cost and logistics of
vaccines are associated with keeping therapeutics refrigerated and nearly half
of all vaccines are lost due to breaks in the cold chain. Relief programs,
thus, struggle to maintain vaccine viability. To mitigate the reliance on the
cold chain, vaccines and other temperature-dependent therapeutics need to be
stabilized against higher temperatures. Complex coacervation is a liquid-liquid
phase separation phenomenon that offers a novel means of encapsulating
biologics similar to how proteins are found in their native milieu. We
hypothesize that this biomimicry will thermally stabilize these moieties and
lower the dependence on the cold chain. Additionally, this process is entirely
aqueous and is biologically compatible. Previous work has shown that proteins can
be effectively incorporated into complex coacervates at high loadings. We have
investigated the effect of various parameters such as protein charge, polymer
charge density, and polymer charge sequence on the encapsulation of a number of
model proteins including bovine serum albumin, hen egg white lysozyme, and a
monoclonal antibody using poly(lysine) and poly(glutamate)-based
complex coacervates. Furthermore, we have examined the trends in both
coacervate formation and protein incorporation as a function of the composition
of the ternary polycation, polyanion, protein mixture.
Optimization of coacervation conditions can facilitate a more than 1000-fold
increase in protein concentration compared with the initial solution. These
results suggest the potential for using complex coacervation as a strategy for
the delivery of vaccines and other biologics at high concentrations for a wide
range of applications.
vaccines are associated with keeping therapeutics refrigerated and nearly half
of all vaccines are lost due to breaks in the cold chain. Relief programs,
thus, struggle to maintain vaccine viability. To mitigate the reliance on the
cold chain, vaccines and other temperature-dependent therapeutics need to be
stabilized against higher temperatures. Complex coacervation is a liquid-liquid
phase separation phenomenon that offers a novel means of encapsulating
biologics similar to how proteins are found in their native milieu. We
hypothesize that this biomimicry will thermally stabilize these moieties and
lower the dependence on the cold chain. Additionally, this process is entirely
aqueous and is biologically compatible. Previous work has shown that proteins can
be effectively incorporated into complex coacervates at high loadings. We have
investigated the effect of various parameters such as protein charge, polymer
charge density, and polymer charge sequence on the encapsulation of a number of
model proteins including bovine serum albumin, hen egg white lysozyme, and a
monoclonal antibody using poly(lysine) and poly(glutamate)-based
complex coacervates. Furthermore, we have examined the trends in both
coacervate formation and protein incorporation as a function of the composition
of the ternary polycation, polyanion, protein mixture.
Optimization of coacervation conditions can facilitate a more than 1000-fold
increase in protein concentration compared with the initial solution. These
results suggest the potential for using complex coacervation as a strategy for
the delivery of vaccines and other biologics at high concentrations for a wide
range of applications.