Han, R, Maycock, J, Murray, BS et al. (1 more author) (2019) Identification of angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory peptides derived from oilseed proteins using two integrated bioinformatic approaches. Food Research International, 115. pp. 283-291. ISSN 0963-9969
Abstract
Angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) play critical roles in the development of hypertension and type 2 diabetes, respectively. Inhibiting ACE and DPP-IV activity using peptides has become part of new therapeutic strategies for supporting medicinal treatment of both diseases. In this study, oilseed proteins, including soybean, flaxseed, rapeseed, sunflower and sesame are evaluated for the possibility of generating ACE and DPP-IV inhibitory peptides using different integrated bioinformatic approaches (UniProt knowledgebase, ProtParam, BLAST, BIOPEP, PeptideRanker, Pepsite2 and ToxinPred), and three bovine proteins (β-lactoglobulin, β-casein and κ-casein) as comparisons. Compared with bovine proteins, the potency indices of ACE and DPP-IV inhibitory peptides, calculated using the BIOPEP database, suggest that oilseed proteins may be considered as good precursors of ACE inhibitory peptides but generate a relative lower yield of DPP-IV inhibitory peptides following subtilisin, pepsin (pH = 1.3) or pepsin (pH > 2) hydrolysis. Average scores aligned using PeptideRanker confirmed oilseed proteins as significant potential sources of bioactive peptides: over 105 peptides scored over 0.8. Pepsite2 predicted that these peptides would largely bind via Gln281, His353, Lys511, His513, Tyr520 and Tyr523 of ACE to inhibit the enzyme, while Trp629 would be the predominant binding site of peptides in reducing DPP-IV activity. All peptides were capable of inhibiting ACE and DPP-IV whilst 65 of these 105 peptides are not currently recorded in BIOPEP database. In conclusion, our in silico study demonstrates that oilseed proteins could be considered as good precursors of ACE and DPP-IV inhibitory peptides as well as so far unexplored peptides that potentially have roles in ACE and DPP-IV inhibition and beyond.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 Published by Elsevier Ltd. This is an author produced version of a paper published in Food Research International. Uploaded in accordance with the publisher's self-archiving policy |
Keywords: | Angiotensin-converting enzyme; Dipeptidyl peptidase-IVBioactive peptides; Hypertension; Diabetes; Bioinformatics; in silico analysis; Oilseed proteins |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Environment (Leeds) > School of Food Science and Nutrition (Leeds) > FSN Chemistry and Biochemistry (Leeds) The University of Leeds > Faculty of Environment (Leeds) > School of Food Science and Nutrition (Leeds) > FSN Nutrition and Public Health (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 10 Jan 2019 13:52 |
Last Modified: | 12 Dec 2019 01:39 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.foodres.2018.12.015 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:140835 |
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Filename: R Han Manuscript FRI In silico final repository_.pdf
Licence: CC-BY-NC-ND 4.0