Marrleisy, D and Lahiri, K and Balaram, P (1985) Bilirubin binding to polypeptides and chiral amines. Induced circular dichroism and fluorescence studies. In: International Journal of Peptide and Protein Research, 25 (3). 290 -296.
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Induced Cotton effects have been observed in the visible region on interaction of bilirubin with chiral mono- and diamines and poly-l-lysine. At alkaline pH distinct CD spectra are observed for bilirubin bound to the α-helical and β-sheet conformation of poly-l-lysine, which differ from that observed for the pigment bound to human serum albumin. The CD pattern observed on binding to N-acetyl-Lys-N1-methylamide in CH2Cl2 and dioxane is different from that observed in the presence of l-Ala-NH-(CH2)6-NH-l-Ala in dioxane. The latter case resembles the spectrum observed in the presence of human serum albumin. Binding to the helical polypeptide melittin and the antiparallel β-sheet peptide, gramicidin S, in aqueous solutions results in opposite signs of the bilirubin CD bands. The quenching of tryptophan fluorescence in melittin, in aqueous solution and enhancement of bilirubin fluorescence in dioxane on binding to gramicidin S have been used to monitor pigment-peptide interactions. The results suggest the utility of bilirubin as a conformational probe.
| Item Type: | Journal Article |
|---|---|
| Publication: | International Journal of Peptide and Protein Research |
| Publisher: | Munksgaard (Wiley) |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 29 Jul 2009 03:06 |
| Last Modified: | 29 Jul 2009 03:06 |
| URI: | http://eprints.iisc.ac.in/id/eprint/21851 |
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