Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed
Inhibitor of α-amylase offers an effective strategy to modulate hyperglycemia. Three novel cumin-seed peptides (CSPs) were proposed as potent inhibitors according to previous study. This study was performed to further assess the clinical relevance of CSPs in simulated physiological conditions via an...
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doaj-4a4a4ccdb14c443c8e2a09a0fc8f36532021-04-30T07:10:40ZengElsevierJournal of Functional Foods1756-46462017-08-0135216223Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seedHwee-Leng Siow0Gee-Jun Tye1Chee-Yuen Gan2Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, 11800 USM, Penang, MalaysiaInstitute for Research in Molecular Medicine, Universiti Sains Malaysia, 11800 USM, Penang, Malaysia; Corresponding author.Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, 11800 USM, Penang, Malaysia; Corresponding author.Inhibitor of α-amylase offers an effective strategy to modulate hyperglycemia. Three novel cumin-seed peptides (CSPs) were proposed as potent inhibitors according to previous study. This study was performed to further assess the clinical relevance of CSPs in simulated physiological conditions via an in vitro model using AR42J α-amylase secretory cells. The CSPs displayed dose-dependent manners for bioactivities and cytotoxic responses. The IC50 values for inhibition were 5.6, 1.58, and 2.39 mg/ml, for CSP3, CSP4 and CSP6, respectively. The following starch load test further confirmed the efficiencies of CSPs as potent α-amylase inhibitor, as they were found capable of retaining more than 50% of their initial inhibition upon 2 h treatment. In addition, CSPs displayed mixed-type inhibition patterns with respect to soluble substrate (∼7.3–29.2 mM), suggesting that these peptide inhibitors have multiple binding modes to α-amylase. Therefore, CSPs exhibit promising potentials for development as new agents for the treatment of diabetic.http://www.sciencedirect.com/science/article/pii/S1756464617302943α-Amylase inhibitionBioactive peptidesCumin seedCell-based assayEnzyme kinetics |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Hwee-Leng Siow Gee-Jun Tye Chee-Yuen Gan |
spellingShingle |
Hwee-Leng Siow Gee-Jun Tye Chee-Yuen Gan Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed Journal of Functional Foods α-Amylase inhibition Bioactive peptides Cumin seed Cell-based assay Enzyme kinetics |
author_facet |
Hwee-Leng Siow Gee-Jun Tye Chee-Yuen Gan |
author_sort |
Hwee-Leng Siow |
title |
Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed |
title_short |
Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed |
title_full |
Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed |
title_fullStr |
Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed |
title_full_unstemmed |
Pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (Cuminum cyminum) seed |
title_sort |
pre-clinical evidence for the efficacy and safety of α-amylase inhibitory peptides from cumin (cuminum cyminum) seed |
publisher |
Elsevier |
series |
Journal of Functional Foods |
issn |
1756-4646 |
publishDate |
2017-08-01 |
description |
Inhibitor of α-amylase offers an effective strategy to modulate hyperglycemia. Three novel cumin-seed peptides (CSPs) were proposed as potent inhibitors according to previous study. This study was performed to further assess the clinical relevance of CSPs in simulated physiological conditions via an in vitro model using AR42J α-amylase secretory cells. The CSPs displayed dose-dependent manners for bioactivities and cytotoxic responses. The IC50 values for inhibition were 5.6, 1.58, and 2.39 mg/ml, for CSP3, CSP4 and CSP6, respectively. The following starch load test further confirmed the efficiencies of CSPs as potent α-amylase inhibitor, as they were found capable of retaining more than 50% of their initial inhibition upon 2 h treatment. In addition, CSPs displayed mixed-type inhibition patterns with respect to soluble substrate (∼7.3–29.2 mM), suggesting that these peptide inhibitors have multiple binding modes to α-amylase. Therefore, CSPs exhibit promising potentials for development as new agents for the treatment of diabetic. |
topic |
α-Amylase inhibition Bioactive peptides Cumin seed Cell-based assay Enzyme kinetics |
url |
http://www.sciencedirect.com/science/article/pii/S1756464617302943 |
work_keys_str_mv |
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