Abstract
Three novel antioxidative and amylase inhibitor peptides were identified from the Basil seeds. The bioactivities were determined based on 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical scavenging activity, ferric reducing antioxidant power and α-amylase inhibitory activity. The peptide sequences were identified using LC/MS LTQ-Orbitrap. The identified peptides were: P1 (ACGNLPRMC), P2 (ACNLPRMC) and P3 (AGCGCEAMFAGA). According to the in silico structural model, these peptides were bound to the substrate binding residues (Trp58, Trp59, Tyr62, Val163, His299, Asp300 and His305) and catalytic residue (Asp300) of α-amylase with their active fragments (i.e. Asn-Leu-Pro-Arg-Met-Cys of P1 and P2, and Met-Phe-Ala-Gly-Ala of P3). Thus, a low number of subsites and the architectural modification of active site of α-amylase occurred. The flexibility of the α-amylase were restricted and could not adopt the conformation to adapt the carbohydrate, and thus interfered the formation of glycosyl-enzyme intermediate. In terms of antioxidative property, the peptides were able to donate electrons in order to quench free radicals and terminate the radical chain reaction.
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This project was funded by RUI Grant (1001/CAATS/814257).
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Nurul Hidayatul Afifah, B.S.S., Gan, CY. Antioxidative and Amylase Inhibitor Peptides from Basil Seeds. Int J Pept Res Ther 22, 3–10 (2016). https://doi.org/10.1007/s10989-015-9477-5
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DOI: https://doi.org/10.1007/s10989-015-9477-5