publication . Article . 2008

Study of protein conformational stability and integrity using calorimetry and FT-Raman spectroscopy correlated with enzymatic activity

Elkordy, Amal; Forbes, Robert T; Barry, Brian W;
Open Access
  • Published: 05 Feb 2008 Journal: European Journal of Pharmaceutical Sciences, volume 33, pages 177-190 (issn: 0928-0987, Copyright policy)
  • Publisher: Elsevier BV
  • Country: United Kingdom
Abstract
Abstract Maintaining protein conformational stability and integrity during formulation is critical for developing protein pharmaceuticals. Accordingly, high sensitivity differential scanning calorimetry (HSDSC) and Fourier transform (FT)-Raman spectroscopy were employed to assess conformational stabilities (thermal stability and folding reversibility) and structural integrities, respectively, for three model proteins: lysozyme, deoxyribonuclease I (DNase I) and lactate dehydrogenase (LDH) in lyophilised (as received) and spray-dried forms. Enzymatic assay after cooling of thermally denatured protein solutions from HSDSC determined if thermal transition reversibi...
Subjects
free text keywords: Pharmaceutical Science, Biochemistry, Enzyme, chemistry.chemical_classification, chemistry, Deoxyribonuclease I, Chromatography, Protein secondary structure, Differential scanning calorimetry, Calorimetry, Thermal stability, Lysozyme, chemistry.chemical_compound, Denaturation (biochemistry), sub_chemistry
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publication . Article . 2008

Study of protein conformational stability and integrity using calorimetry and FT-Raman spectroscopy correlated with enzymatic activity

Elkordy, Amal; Forbes, Robert T; Barry, Brian W;