抄録
Amorphous matrices formed by sugars are widely used as bulk-forming agents, stabilizing agents for physically/chemically labile ingredients such as proteins in the drug manufacturing industries. The intermolecular interactions involved in the amorphous sugar matrix closely relate to the physical properties of the amorphous sugar matrix: Hydrogen bonds among sugar molecules largely contribute to holding the amorphous sugar matrix in the solid state; The interactions between sugar and substances embedded in the sugar matrix (polymer, salts etc.) significantly affect the physical stability of the amorphous matrix; In the sugar-protein mixture, the sugar-protein hydrogen bonds play an essential role in the stabilization of protein. In this study, the intermolecular interactions in amorphous sugar matrices and the mixtures with polymer additive (polyvinylpyrrolidone, PVP) and protein were analyzed using temperature scanning Fourier transform infrared spectroscopy, TS-FTIR. From the investigations, the following findings were obtained: 1) The amorphous sugar matrix, in which sugar molecules can be fixed by fewer hydrogen bonds, has a higher glass transition temperature (Tg). 2) The heat-induced conformational changes of proteins were significant at temperatures above the glass transition temperature. 3) The addition of PVP to amorphous matrix tended to prevent the disruption of hydrogen bonds due to increasing temperature.
https://ror.org/02pc6pc55 
