We studied seven known peptides derived from different food proteins， and one hydrophobic peptide derived through in-silico hydrolysis. We investigated their antioxidative， antimicrobial and haemolytic activities and their interactions with model lipid membranes. Our data reveal that peptides with histidines are the most effective for protection against lipid peroxidation， as: P#3 (VHHA) > P#5 (LHALLL) > P#7 (LLPHH). The most potent peptide towards metal-induced oxidation was P#2 (LQKW)， which contained an aromatic tryptophan at its C-terminus. The peptides with negative hydrophobicity， as P#1 (PEL) and P#2 (LQKW)， were the most potent according to DPPH radical scavenging. The most potent peptide towards superoxide radicals was the four-amino-acid chain with aromatic amino acids， P#2 (LQKW). The peptides studied did not show haemolytic or antimicrobial activities， except P#4 (AAGGV) against Listeria monocytogenes. These peptides did not interact with model lipid membranes， except P#8， which was designed to span lipid bilayers.