Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state

Glass dynamics as measured by τ could not explain the stability results. Stability correlated best with the preservation of native structure for sucrose-based formulations, but with the trehalose-based formulation, neither structural relaxation time nor extent of native structure was predictive of stability. However, it is possible that the β-relaxations rather than the α-relaxation (i.e., the τ we measured) is critical to the stability. Plasticizers like glycerol may decrease τ for “α-motion” but increase τ for “β-motion” and stabilize proteins (Cicerone MT, Tellington A, Trost L, Sokolov A, 2003, BioProcess Inter 1:1-9). © 2005 Wiley-Liss, Inc. and the American Pharmacists Association