Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance

complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from chicken ovalbumin (OVA). This approach involved PeptideCutter, Peptide Ranker and Pepsite2 in order to hydrolyse OVA protein sequence...

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Main Author: Mohd Salim, Mohd Adam
Format: Thesis
Language:English
Published: 2021
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Online Access:http://eprints.usm.my/53229/1/MOHD%20ADAM%20SALIM%20BIN%20MOHD%20SALIM%20-%20TESIS24.pdf
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spelling my-usm-ep.532292022-06-30T17:34:06Z Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance 2021-10 Mohd Salim, Mohd Adam QD415-436 Biochemistry complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from chicken ovalbumin (OVA). This approach involved PeptideCutter, Peptide Ranker and Pepsite2 in order to hydrolyse OVA protein sequence into smaller peptides, to identify the probability of the peptides being bioactive and to investigate the interaction between the peptides and target enzymes (i.e. ACE and DPP-4), respectively. OVA sequence was initially hydrolysed using PeptideCutter. Pepsin (P), Chymotrypsin (C) and Trypsin (T) were used in 7 different OVA (O) hydrolysis combination (OP, OC, OT, OCT, OPC, OPT and OPCT), thus, producing 71 peptides. Top ten novel bioactive peptides (i.e. CF, KM, ELPF, AM, ADHPH, LPR, PR, FR, PRM and GR) were then successfully identified and selected based on the amino acid sequences as well as the peptide interactions with ACE and DPP-4. Against ACE, IC50 of CF, KM, ELPF, AM, ADHPH, LPR, PR, FR, PRM and GR were 1.82, 1.89, 4.24, 3.07, 3.54, 1.30, 5.47, 4.35, 5.22 and 3.11 mM, respectively. These results were comparable to commercial inhibitor for ACE, captopril (IC50 = 3.98 mM). While against DPP-4, however, inhibitory activities were only comparable to other reported DPP-4 inhibitory peptides such as EK (IC50 = 3.22 mM) and GL (IC50 = 2.62 mM), as the peptides were able to achieve 2.99, 2.22, 9.92, 2.79, 1.66, 1.43, 4.11, 2.47, 2.50 and 2.83 mM, respectively 2021-10 Thesis http://eprints.usm.my/53229/ http://eprints.usm.my/53229/1/MOHD%20ADAM%20SALIM%20BIN%20MOHD%20SALIM%20-%20TESIS24.pdf application/pdf en public masters Universiti Sains Malaysia. Pusat Penyelidikan Biokimia Analisis
institution Universiti Sains Malaysia
collection USM Institutional Repository
language English
topic QD415-436 Biochemistry
spellingShingle QD415-436 Biochemistry
Mohd Salim, Mohd Adam
Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
description complete integrated bioinformatics approach was developed to identify angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-4 (DPP-4) inhibitory peptides from chicken ovalbumin (OVA). This approach involved PeptideCutter, Peptide Ranker and Pepsite2 in order to hydrolyse OVA protein sequence into smaller peptides, to identify the probability of the peptides being bioactive and to investigate the interaction between the peptides and target enzymes (i.e. ACE and DPP-4), respectively. OVA sequence was initially hydrolysed using PeptideCutter. Pepsin (P), Chymotrypsin (C) and Trypsin (T) were used in 7 different OVA (O) hydrolysis combination (OP, OC, OT, OCT, OPC, OPT and OPCT), thus, producing 71 peptides. Top ten novel bioactive peptides (i.e. CF, KM, ELPF, AM, ADHPH, LPR, PR, FR, PRM and GR) were then successfully identified and selected based on the amino acid sequences as well as the peptide interactions with ACE and DPP-4. Against ACE, IC50 of CF, KM, ELPF, AM, ADHPH, LPR, PR, FR, PRM and GR were 1.82, 1.89, 4.24, 3.07, 3.54, 1.30, 5.47, 4.35, 5.22 and 3.11 mM, respectively. These results were comparable to commercial inhibitor for ACE, captopril (IC50 = 3.98 mM). While against DPP-4, however, inhibitory activities were only comparable to other reported DPP-4 inhibitory peptides such as EK (IC50 = 3.22 mM) and GL (IC50 = 2.62 mM), as the peptides were able to achieve 2.99, 2.22, 9.92, 2.79, 1.66, 1.43, 4.11, 2.47, 2.50 and 2.83 mM, respectively
format Thesis
qualification_level Master's degree
author Mohd Salim, Mohd Adam
author_facet Mohd Salim, Mohd Adam
author_sort Mohd Salim, Mohd Adam
title Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
title_short Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
title_full Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
title_fullStr Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
title_full_unstemmed Identification Of Bioactive Peptide From Chicken Ovalbumin Using An Integrated Bioinformatics-assisted Approach And Determining Their Functional Significance
title_sort identification of bioactive peptide from chicken ovalbumin using an integrated bioinformatics-assisted approach and determining their functional significance
granting_institution Universiti Sains Malaysia.
granting_department Pusat Penyelidikan Biokimia Analisis
publishDate 2021
url http://eprints.usm.my/53229/1/MOHD%20ADAM%20SALIM%20BIN%20MOHD%20SALIM%20-%20TESIS24.pdf
_version_ 1747822231963041792