Hydrogen Bonding Interactions and Enthalpy Relaxation in Sugar/Protein Glasses

In this study, hydrogen bonding interactions and enthalpy relaxation phenomena of sugar and sugar/protein glasses have been studied using Fourier transform infrared spectroscopy and differential scanning calorimetry. The sugar OH band in Fourier transform infrared spectra was used to derive the glas...

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Veröffentlicht in:	Journal of pharmaceutical sciences 2017-03, Vol.106 (3), p.761-769
Hauptverfasser:	Sydykov, Bulat, Oldenhof, Harriëtte, Sieme, Harald, Wolkers, Willem F.
Format:	Artikel
Sprache:	eng
Schlagworte:	amorphous Animals calorimetry (DSC) Cattle Disaccharides - chemistry Disaccharides - metabolism FTIR glass Glass - chemistry Hydrogen Bonding Monosaccharides - chemistry Monosaccharides - metabolism proteins Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - metabolism Spectroscopy, Fourier Transform Infrared - methods stability Sugars - chemistry Sugars - metabolism Thermodynamics Transition Temperature
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