Application of ATR‐FTIR spectroscopy to the study of thermally induced changes in secondary structure of protein molecules in solid state

• DOI: 10.1002/bip.22664
• Publication Date: 2015-04-29T20:53:11Z
• Authors: Jorge Cruz‐Angeles; Luz María Martínez; Marcelo Videa
• Keywords: Biomolecule; Denaturation (fissile materials); Thermal Treatment

FTIR spectroscopy in combination with ATR sampling technique is the most accessible analytical to study secondary structure of proteins both solid and aqueous solution. Although several studies have demonstrated applications ATR-FTIR conformational changes dried due dehydration, there are no reports that demonstrate application thermally induced biomolecules directly on state. In this study, four pharmaceutical interest, lysozyme, myoglobine, chymotripsin human growth hormone (hGH), were studied state before after different thermal treatments order relate partial or total denaturation processes. The results obtained provide experimental evidence protein can be detected by displacement carbonyl bands which correspond transformations between α-helix β-sheet intermolecular β-sheet; molecules undergo transformation when exposed a temperature close their may become irreversible depending extent heating treatment. These findings an effective time efficient allows monitoring process samples without further reconstitution prior sample preparation.