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

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Keywords amide II′, antioxidant peptide, proline, UV resonance Raman
Persistent URL dx.doi.org/10.1002/jrs.2971
Journal Journal of Raman Spectroscopy
Citation
Pripotnev, S. (Stahs), Tsopmo, A, Friel, J.K. (James K.), & Ianoul, A.I. (2011). UV resonance Raman spectroscopy probes the amide II′p band position in short breast milk peptides with antioxidant activity. Journal of Raman Spectroscopy, 42(12), 2105–2111. doi:10.1002/jrs.2971