Kyle Cole - Ultra-Stable Hemoglobin–Poly(Acrylic Acid) Conjugates

Document created by Kyle Cole on Aug 22, 2014
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  Publication Details (including relevant citation   information):

J. Mater. Chem., 2012,22, 20423-20433


  Stabilization   of proteins against thermal deactivation is a major challenge,   and a simple, facile, novel chemical approach is described here   to overcome this hurdle. We report here, for the first time, the   successful synthesis of ultrastable protein nanoparticles   consisting of met-hemoglobin (Hb) conjugated with low molecular   weight polyacrylic acid (PAA, Mw  8000) to   form discrete nanoparticles. Hb–PAA nanoparticles were not   deactivated when subjected to prolonged thermal treatment such as   steam sterilization conditions (122 °C, 40 minutes, 17–20 psi),   while the unprotected Hb lost most of its activity when subjected   to the same heating conditions. Several Hb–PAA derivatives which   resist thermal inactivation, in a similar manner, are produced   and characterized. Interestingly, the highest activity retention,   after the above thermal treatment, was [similar]100%   for the untreated samples. This resistance to heat is attributed   to the enhanced thermodynamic stability of the Hb–PAA conjugate   and improved re-folding of the denatured state to the native   form, facilitated by PAA conjugation to Hb. This is a unique   approach to stabilize Hb against thermal inactivation, and it is   a major breakthrough in the production of stable Hb-based   nanomaterials that can be safely sterilized in an autoclave for   biomedical/in   vivo applications.

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