Structural determinants of the immunomodulatory properties of the C-terminal region of bovine ß-casein

TY - JOUR

T1 - Structural determinants of the immunomodulatory properties of the C-terminal region of bovine ß-casein

AU - Bonomi, Francesco

AU - Brandt, Rikke

AU - Favalli, Sara

AU - Ferranti, Pasquale

AU - Fierro, Olga

AU - Frøkiær, Hanne

AU - Ragg, Enzio

AU - Iamettia, Stefania

PY - 2011/10

Y1 - 2011/10

N2 - 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.

AB - 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.

U2 - 10.1016/j.idairyj.2011.04.012

DO - 10.1016/j.idairyj.2011.04.012

M3 - Journal article

SN - 0958-6946

VL - 21

SP - 770

EP - 776

JO - International Dairy Journal

JF - International Dairy Journal

IS - 10

ER -