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Chemical synthesis and structure elucidation of bovine K-casein (1-44)

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Bansal, P.S., Daly, N.L., McGhie, E., Craik, D.J., Alewood, P.F., Grieve, P. and Marschke, R.J. (2006) Chemical synthesis and structure elucidation of bovine K-casein (1-44). Biochemical and Biophysical Research Communications, 340 (4). pp. 1098-1103.

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Article Link: http://dx.doi.org/10.1016/j.bbrc.2005.12.115

Publisher URL: http://www.elsevier.com


The caseins (αs1, αs2, β, and κ) are phosphoproteins present in bovine milk that have been studied for over a century and whose structures remain obscure. Here we describe the chemical synthesis and structure elucidation of the N-terminal segment (1–44) of bovine κ-casein, the protein which maintains the micellar structure of the caseins. κ-Casein (1–44) was synthesised by highly optimised Boc solid-phase peptide chemistry and characterised by mass spectrometry. Structure elucidation was carried out by circular dichroism and nuclear magnetic resonance spectroscopy. CD analysis demonstrated that the segment was ill defined in aqueous medium but in 30% trifluoroethanol it exhibited considerable helical structure. Further, NMR analysis showed the presence of a helical segment containing 26 residues which extends from Pro8 to Arg34. This is the first report which demonstrates extensive secondary structure within the casein class of proteins.

Item Type:Article
Corporate Creators:Emerging Technologies, Department of Employment, Economic Development and Innovation (DEEDI), Crop and Food Science , Agri-Science
Business groups:Crop and Food Science
Additional Information:© Elsevier.
Keywords:K-Casein; 2D NMR; helical structure; milk protein; solid phase peptide synthesis.
Subjects:Animal culture > Cattle > Dairy processing. Dairy products
Agriculture > Agriculture (General) > Agricultural chemistry. Agricultural chemicals
Live Archive:18 Nov 2008 05:06
Last Modified:03 Sep 2021 16:43

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