Peptide mixtures prepared from soybean β-conglycinin (7S-peptides) were acylated with saturated fatty acids of different chain length (6C-18C) in order to improve their antiviral activity against Feline calicivirus (FCV) strain F9 which is a typical norovirus surrogate. Among the fatty acids varieties, it was revealed that 7S-peptides acylated with myristic and palmitic acids potently inhibited FCV replication. Myristorylation and palmitoylation of 7S-peptides kept host cells viability at 91.51% and 98.90%, respectively. The infectivity of FCV on Crandell-Reese feline kidney cells was further determined after exposure of initial titer of 10(6.47) TCID₅₀/mL. Myristoylated and palmitoylated 7S-peptides significantly (P < 0.006) reduced FCV infectivity as compared to native 7S-peptides. Native 7S-peptides showed 25% FCV inhibitory activity while myristoylated and palmitoylated 7S-peptides exhibited 98.59% and 99.98% reduction in FCV infectivity, respectively. Myristoylated and palmitoylated 7S-peptides demonstrated higher anti-FCV activity in a wide range of concentration with complete reduction at 25 μg/mL. Surface hydrophobicity was significantly (P < 0.05) increased after attachment of long hydrocarbon fatty acids to 7S-peptides as supported by changes in fluorescence intensity. Enzymatic hydrolysis together with acylation will give an insight into surface and physiological functional lipopeptides derived from soy β-conglycinin.
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