Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay
A complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from egg white ovalbumin. The sequence of the protein was initially obtained from the NCBI database followed by in silico digestion using...
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doaj-eac4d4d3a72147eabb1f2544dc0befd22021-04-30T07:17:36ZengElsevierJournal of Functional Foods1756-46462020-01-0164103618Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assayMohd Adam Salim Mohd Salim0Chee-Yuen Gan1Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, 11800 USM Penang, MalaysiaCorresponding author.; Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, 11800 USM Penang, MalaysiaA complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from egg white ovalbumin. The sequence of the protein was initially obtained from the NCBI database followed by in silico digestion using different enzymes or combination of enzymes. The results showed that 71 peptides were produced. Their bioactivities were then predicted based on the amino acid compositions and sequences as well as the peptide interactions with ACE and DPP-4. Ten highly potential peptides (CF, KM, ELPF, AM, ADHPF, LPR, PR, FR, PRM and GR) were chosen as they obtained p-value less than 0.01. The results from the in vitro validation experiment showed that all peptides were able to inhibit the ACE and DPP-4. Overall, this study underlined the in silico approach as an alternative way for bioactive peptide discovery which could tremendously reduce the cost and time of research.http://www.sciencedirect.com/science/article/pii/S1756464619305420ACE inhibitory peptideDPP-4 inhibitory peptideEgg whiteIn silico analysisOvalbumin |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mohd Adam Salim Mohd Salim Chee-Yuen Gan |
spellingShingle |
Mohd Adam Salim Mohd Salim Chee-Yuen Gan Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay Journal of Functional Foods ACE inhibitory peptide DPP-4 inhibitory peptide Egg white In silico analysis Ovalbumin |
author_facet |
Mohd Adam Salim Mohd Salim Chee-Yuen Gan |
author_sort |
Mohd Adam Salim Mohd Salim |
title |
Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay |
title_short |
Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay |
title_full |
Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay |
title_fullStr |
Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay |
title_full_unstemmed |
Dual-function peptides derived from egg white ovalbumin: Bioinformatics identification with validation using in vitro assay |
title_sort |
dual-function peptides derived from egg white ovalbumin: bioinformatics identification with validation using in vitro assay |
publisher |
Elsevier |
series |
Journal of Functional Foods |
issn |
1756-4646 |
publishDate |
2020-01-01 |
description |
A complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from egg white ovalbumin. The sequence of the protein was initially obtained from the NCBI database followed by in silico digestion using different enzymes or combination of enzymes. The results showed that 71 peptides were produced. Their bioactivities were then predicted based on the amino acid compositions and sequences as well as the peptide interactions with ACE and DPP-4. Ten highly potential peptides (CF, KM, ELPF, AM, ADHPF, LPR, PR, FR, PRM and GR) were chosen as they obtained p-value less than 0.01. The results from the in vitro validation experiment showed that all peptides were able to inhibit the ACE and DPP-4. Overall, this study underlined the in silico approach as an alternative way for bioactive peptide discovery which could tremendously reduce the cost and time of research. |
topic |
ACE inhibitory peptide DPP-4 inhibitory peptide Egg white In silico analysis Ovalbumin |
url |
http://www.sciencedirect.com/science/article/pii/S1756464619305420 |
work_keys_str_mv |
AT mohdadamsalimmohdsalim dualfunctionpeptidesderivedfromeggwhiteovalbuminbioinformaticsidentificationwithvalidationusinginvitroassay AT cheeyuengan dualfunctionpeptidesderivedfromeggwhiteovalbuminbioinformaticsidentificationwithvalidationusinginvitroassay |
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