title: Inhibition of proteolysis in oxidized lipid-damaged proteins.
abstract: The proteolysis of bovine serum albumin (BSA) modified by reaction with the lipid peroxidation product 4,5(E)-epoxy-2(E)-heptenal was studied to better understand the loss of digestibility observed in oxidized lipid-damaged proteins. BSA was incubated for different periods of time with eight concentrations of the epoxyalkenal and, then, treated for 24 h with chymotrypsin, pancreatin, Pronase, or trypsin. The treatment of BSA with the aldehyde always decreased its proteolysis in relation to that of native BSA, and this inhibition of the proteolysis was related to the concentration of the epoxyalkenal and the reaction time. In fact, this inhibition was correlated with the damage suffered by the protein as a consequence of its reaction with the aldehyde: mainly the development of browning, the denaturation of the protein, and the formation of the oxidized lipid/amino acid reaction product epsilon-N-pyrrolylnorleucine (p < or = 0.0011, 0.0045, and 0.0031, respectively). In addition, epsilon-N-pyrrolylnorleucine added at 0.1 or 1 mM inhibited the proteases assayed and suggested that the inhibition of the proteolysis observed in oxidized lipid-damaged proteins may be related to the formation and accumulation of pyrrolized amino acid residues.
authors.affiliation: Instituto de la Grasa, CSIC, Avenida Padre García Tejero 4, 41012 Sevilla, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Zamora
authors.forename: F J
authors.initials: FJ
authors.lastname: Hidalgo
mesh_terms: D000447:Aldehydes; D002918:Chymotrypsin / Q000378:metabolism; D004852:Epoxy Compounds; D006868:Hydrolysis; D007700:Kinetics; D015227:Lipid Peroxidation; D009646:Norleucine / Q000031:analogs & derivatives*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013997:Time Factors
chemical_list: C095287:6-pyrrolylnorleucine; D000447:Aldehydes; D004852:Epoxy Compounds; D012710:Serum Albumin, Bovine; C082505:4,5-epoxy-2-heptenal; D009646:Norleucine; D002918:Chymotrypsin