Peptides derived from digestive or cellular degradation of food proteins have been studied for they affect a number of biochemical responses in human, including systemic ones. Caseins are among the prime sources of the so called “bioactive peptides”. The immunomodulating activity of synthetic peptides corresponding to the C-terminal sequence of bovine beta-casein was measured in a splenocyte proliferation assay, and compared with structural information from CD and NMR studies. Immunosuppressory activity required the minimal sequence (203-209) GPFPIIV, and was absent when L-Pro at P206 was substituted by D-Pro. This substitution results in loss of the structural features of this peptide, that cannot be relieved by introducing the arginine residue at position 202. However, peptides that include the hydrophobic stretch (194-201) YQQPVLGPV were active and structured, even when P206 was substituted by the structural homologues of proline, INP and THZ. These results point to a structure-function relationship in casein-derived peptides, and indicates that even the smallest peptides may have biological activities, once their structural identity is preserved.

Structural determinants of the immunoregulatory activity of milk-derived peptides : the C-terminal sequences of bovine beta-casein / S. Iametti, A. Barbiroli, E. Ragg, P. Ferranti, O. Fierro, S. Favalli, H. Frokiaer, F. Bonomi. ((Intervento presentato al 54. convegno National Meeting of the Italian Society of Biochemistry and Molecular Biology tenutosi a Catania (Italy) nel 2009.

Structural determinants of the immunoregulatory activity of milk-derived peptides : the C-terminal sequences of bovine beta-casein

S. Iametti
Primo
;
A. Barbiroli
Secondo
;
E. Ragg;F. Bonomi
Ultimo
2009

Abstract

Peptides derived from digestive or cellular degradation of food proteins have been studied for they affect a number of biochemical responses in human, including systemic ones. Caseins are among the prime sources of the so called “bioactive peptides”. The immunomodulating activity of synthetic peptides corresponding to the C-terminal sequence of bovine beta-casein was measured in a splenocyte proliferation assay, and compared with structural information from CD and NMR studies. Immunosuppressory activity required the minimal sequence (203-209) GPFPIIV, and was absent when L-Pro at P206 was substituted by D-Pro. This substitution results in loss of the structural features of this peptide, that cannot be relieved by introducing the arginine residue at position 202. However, peptides that include the hydrophobic stretch (194-201) YQQPVLGPV were active and structured, even when P206 was substituted by the structural homologues of proline, INP and THZ. These results point to a structure-function relationship in casein-derived peptides, and indicates that even the smallest peptides may have biological activities, once their structural identity is preserved.
set-2009
Settore BIO/10 - Biochimica
Settore CHIM/06 - Chimica Organica
Structural determinants of the immunoregulatory activity of milk-derived peptides : the C-terminal sequences of bovine beta-casein / S. Iametti, A. Barbiroli, E. Ragg, P. Ferranti, O. Fierro, S. Favalli, H. Frokiaer, F. Bonomi. ((Intervento presentato al 54. convegno National Meeting of the Italian Society of Biochemistry and Molecular Biology tenutosi a Catania (Italy) nel 2009.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/67735
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