This investigation was aimed at the THz spectral components of the product formulation buffer (50.7 mg/mL Mannitol, 25 mM NaPhos, pH7.2), the vaccine adjuvant GPI-0100, and the TA-CIN fusion protein; both separately and in combination. GPI-100 and TA-CIN samples were prepared in the mannitol buffer formulation. TA-CIN is a recombinant HPV vaccine candidate fusion protein containing 726 non-glycosylated amino acids from the L2, E7, and E6 domains of HPV-16 (~MW is 80 kDa). The protein is cysteine and proline rich and exhibits a large number of structural conformers and is naturally found in an aggregated state, with particles typically 0.5 to 1.5 MDa. Specific interest is to investigate the effect of GPI-0100 on the spectra of TA-CIN. Both TA-CIN and GPI-0100 are 0.2�M (sterile) filterable, however in combination they cannot be filtered. We can find no reason for this change in state � Infrared absorbance spectra and dynamic light scattering show no significant changes. DLS in particular shows no change in the aggregation state of TA-CIN on a mass or scattering intensity basis whether formulated with or without GPI-0100. Therefore, terahertz technique was deployed to solve the intricacies. The THz data indicate that a unique spectra is obtained following TA-CIN formulation with GPI-100 � indicating a differently bound macro-molecular state or micelle is formed. This bolsters the hypothesis that a unique large scale repeating structure is generated � most likely a  micelle-containing structure where the native aggregation potential of TA-CIN is maintaining long-range cohesiveness between micelles.

Terahertz investigation of adjuvant and recombinant HPV vaccine candidate fusion protein

247th National Meeting (2014)

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