Monoclonal antibodies are currently one of the largest classes of drug products on the market because of their high specificity, therapeutic impact, and long in vivo half-life. Immunoglobulin G (IgG) is the most popular type of therapeutic antibody on the market now. Their popular usage has encouraged the discovery of new methods to protect IgG in order to expand its’ usage in distant locations. <i>N</i>-isopropylacrylamide (NiPAm) nanoparticles (NPs) have been used in the past for a variety of different purposes. One of the most recent applications takes advantage of the lower critical solution temperature (LCST) of these NiPAm NPs, which causes the particle to undergo an entropically favored collapse when heated above LCST, and to become water swollen when cooled below LCST. Shea <i>et. al.</i> have taken advantage of this property and discovered that they can alter the affinities of these NiPAm NPs to biomacromolecules by changing temperature, therefore creating NPs that can catch and release their biomacromolecular targets. Based on our knowledge of IgG, we are using lightly crosslinked NiPAm NPs with various amounts of hydrophobic and positively charged acrylamide co-monomers to find NPs with the highest affinity for IgG.

Synthesis of polymer hydrogel nanoparticles as heat protectants for IgG

251st National Meeting (2016)

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