Bovine β-casein and its C-terminal sequence (191-209) were previously shown to possess immunomodulatory properties in studies on partially purified peptides from hydrolysates, where minor amounts of contaminants may affect the cellular response. The inhibitory effect of β-casein and of eight C-terminus synthetic β-casein peptides on mitogen-induced spleen cell proliferation was compared. Use of synthetic peptides allowed the unambiguous and accurate identification that a seven amino acid sequence at the C-terminus, including a PFP motif, was sufficient for immunomodulation. Substitution of the last proline (P206) in the PFP motif with D-Pro had a negative impact on the immunosuppressory activity of all these short peptides, whereas substitution of P206 with structural analogues of proline had almost no impact. A relationship was found between the immunomodulatory properties and the structural features of these peptides, as assessed by various spectroscopic approaches, indicating a role of structure in eliciting the immunomodulatory activity of these peptides.
Structural determinants of the immunomodulatory properties of the C-terminal region of bovine β-casein / F. Bonomi, R. Brandt, S. Favalli, P. Ferranti, O. Fierro, H. Frøkiær, E. Ragg, S. Iametti. - In: INTERNATIONAL DAIRY JOURNAL. - ISSN 0958-6946. - 21:10(2011), pp. 770-776.
Structural determinants of the immunomodulatory properties of the C-terminal region of bovine β-casein
F. BonomiPrimo
;E. RaggPenultimo
;S. Iametti
2011
Abstract
Bovine β-casein and its C-terminal sequence (191-209) were previously shown to possess immunomodulatory properties in studies on partially purified peptides from hydrolysates, where minor amounts of contaminants may affect the cellular response. The inhibitory effect of β-casein and of eight C-terminus synthetic β-casein peptides on mitogen-induced spleen cell proliferation was compared. Use of synthetic peptides allowed the unambiguous and accurate identification that a seven amino acid sequence at the C-terminus, including a PFP motif, was sufficient for immunomodulation. Substitution of the last proline (P206) in the PFP motif with D-Pro had a negative impact on the immunosuppressory activity of all these short peptides, whereas substitution of P206 with structural analogues of proline had almost no impact. A relationship was found between the immunomodulatory properties and the structural features of these peptides, as assessed by various spectroscopic approaches, indicating a role of structure in eliciting the immunomodulatory activity of these peptides.File | Dimensione | Formato | |
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