Development of a workflow for screening and identification of α-amylase inhibitory peptides from food source using an integrated Bioinformatics-phage display approach: Case study - Cumin seed
| Autor: | Chee-Yuen Gan, Theam Soon Lim, Hwee-Leng Siow |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Cuminum Phage display In silico Peptide Bioinformatics Hydrolysate Analytical Chemistry Workflow 03 medical and health sciences 0404 agricultural biotechnology Humans Bacteriophages Amylase Amino Acid Sequence Peptide sequence chemistry.chemical_classification biology Computational Biology 04 agricultural and veterinary sciences General Medicine biology.organism_classification 040401 food science Peptide Fragments 030104 developmental biology Biochemistry chemistry Seeds biology.protein alpha-Amylases Alpha-amylase Food Science |
| Zdroj: | Food chemistry. 214 |
| ISSN: | 1873-7072 |
| Popis: | The main objective of this study was to develop an efficient workflow to discover α-amylase inhibitory peptides from cumin seed. A total of 56 unknown peptides was initially found in the cumin seed protein hydrolysate. They were subjected to 2 different in silico screenings and 6 peptides were shortlisted. The peptides were then subjected to in vitro selection using phage display technique and 3 clones (CSP3, CSP4 and CSP6) showed high affinity in binding α-amylase. These clones were subjected to the inhibitory test and only CSP4 and CSP6 exhibited high inhibitory activity. Therefore, these peptides were chemically synthesized for validation purposes. CSP4 exhibited inhibition of bacterial and human salivary α-amylases with IC50 values of 0.11 and 0.04 μmol, respectively, whereas CSP6 was about 0.10 and 0.15 μmol, respectively. Results showed that the strength of each protocol has been successfully combined as deemed fit to enhance the α-amylase inhibitor peptide discovery. |
| Databáze: | OpenAIRE |
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