UV resonance Raman spectroscopy probes the amide II′p band position in short breast milk peptides with antioxidant activity
Article first published online: 2 MAY 2011
Copyright © 2011 John Wiley & Sons, Ltd.
Journal of Raman Spectroscopy
Volume 42, Issue 12, pages 2105–2111, December 2011
How to Cite
Pripotnev, S., Tsopmo, A., Friel, J. K. and Ianoul, A. (2011), UV resonance Raman spectroscopy probes the amide II′p band position in short breast milk peptides with antioxidant activity. J. Raman Spectrosc., 42: 2105–2111. doi: 10.1002/jrs.2971
- Issue published online: 28 DEC 2011
- Article first published online: 2 MAY 2011
- Manuscript Accepted: 24 MAR 2011
- Manuscript Received: 8 FEB 2011
- UV resonance Raman;
- antioxidant peptide;
- amide II′;
UV resonance Raman spectroscopic study of six short proline-containing peptides with antioxidant activity isolated from human breast milk was performed. The amide II′ proline spectroscopic band was used to estimate relative cis trans isomerization state of proline amide bonds in the different peptides. Antioxidant activity of the peptides was determined using 1,1-diphenyl-2-picryl-hydrazyl (DPPH) assay and linoleic acid emulsion assay. Although no clear correlation between the amide II′p position and antioxidant activity of the peptides was observed, they both were found to be sensitive to the presence and/or relative position of proline and tyrosine residues in the peptide. Copyright © 2011 John Wiley & Sons, Ltd.