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Enhanced Antiviral Activity of Soybean β‐Conglycinin‐Derived Peptides by Acylation with Saturated Fatty Acids
Author(s) -
Matemu Athanasia O.,
Nakamura Kosuke,
Kayahara Hisataka,
Murasawa Hisashi,
Katayama Shigeru,
Nakamura Soichiro
Publication year - 2011
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2011.02248.x
Subject(s) - infectivity , chemistry , myristoylation , acylation , palmitoylation , peptide , biochemistry , myristic acid , feline calicivirus , fatty acid , palmitic acid , enzyme , cysteine , virus , biology , membrane , virology , catalysis
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 TCID 50 /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.