A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis
This review focused on assessing the type of amino acids at terminal positions of previously reported DPPIV inhibitory peptides to predict the key feature of sequences that specifically target DPPIV. Thorough understanding on side chain property of reactive amino acids and its contribution on DPPIV...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-10-01
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| Series: | Food Chemistry Advances |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2772753X23000643 |
| _version_ | 1797796084324499456 |
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| author | Ainolsyakira Mohd Rodhi Pei-Gee Yap Olalere Olusegun Abayomi Chee-Yuen Gan |
| author_facet | Ainolsyakira Mohd Rodhi Pei-Gee Yap Olalere Olusegun Abayomi Chee-Yuen Gan |
| author_sort | Ainolsyakira Mohd Rodhi |
| collection | DOAJ |
| description | This review focused on assessing the type of amino acids at terminal positions of previously reported DPPIV inhibitory peptides to predict the key feature of sequences that specifically target DPPIV. Thorough understanding on side chain property of reactive amino acids and its contribution on DPPIV recognition and binding was acquired through structure-activity relationship and molecular docking analysis. Overall, N-terminals dominant by Leu, Pro, Ile, Phe, Ala, Tyr and/or Gly, whereas C-terminals dominant by Arg, Phe, Met, Ala, Val, Pro, Gln, Ile, Glu, Leu and/or Lys depending on the peptide length and terminal positions where these reactive residues hydrophobically interacted with the catalytic (Ser630) or substrate-binding (Tyr629, Tyr547, Tyr666 and Phe357) hotspots of DPPIV. Molecular docking prediction also suggested the presence of secondary hotspots (Arg125, His126, Gly355, Pro359, Ile405, Asp545, Val546, Cys551, Cys552, Gln553, Trp627, Tyr662, Ala707, Asp709, Glu738, Asp739, Gly741, Ile742 and Tyr752) to support peptide binding. In conclusion, outcome of the current review could inspire the design of potent DPPIV inhibitory peptides where the preference for hydrophobic and aliphatic reactive amino acids could be translated into candidate DPPIV-targeting sequences given their ability to engage with DPPIV hotspots. |
| first_indexed | 2024-03-13T03:27:49Z |
| format | Article |
| id | doaj.art-e9c16e6207434508836b1e419c94e392 |
| institution | Directory Open Access Journal |
| issn | 2772-753X |
| language | English |
| last_indexed | 2024-03-13T03:27:49Z |
| publishDate | 2023-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry Advances |
| spelling | doaj.art-e9c16e6207434508836b1e419c94e3922023-06-25T04:44:45ZengElsevierFood Chemistry Advances2772-753X2023-10-012100244A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysisAinolsyakira Mohd Rodhi0Pei-Gee Yap1Olalere Olusegun Abayomi2Chee-Yuen Gan3Analytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM, Lebuh Bukit Jambul, 11900 Bayan Lepas, Penang, MalaysiaAnalytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM, Lebuh Bukit Jambul, 11900 Bayan Lepas, Penang, MalaysiaAnalytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM, Lebuh Bukit Jambul, 11900 Bayan Lepas, Penang, Malaysia; Department of Chemical Engineering, University of Bath, Claverton Down, BA2 7AY Bath, United KingdomAnalytical Biochemistry Research Centre (ABrC), Universiti Sains Malaysia, University Innovation Incubator Building, SAINS@USM, Lebuh Bukit Jambul, 11900 Bayan Lepas, Penang, Malaysia; Corresponding author.This review focused on assessing the type of amino acids at terminal positions of previously reported DPPIV inhibitory peptides to predict the key feature of sequences that specifically target DPPIV. Thorough understanding on side chain property of reactive amino acids and its contribution on DPPIV recognition and binding was acquired through structure-activity relationship and molecular docking analysis. Overall, N-terminals dominant by Leu, Pro, Ile, Phe, Ala, Tyr and/or Gly, whereas C-terminals dominant by Arg, Phe, Met, Ala, Val, Pro, Gln, Ile, Glu, Leu and/or Lys depending on the peptide length and terminal positions where these reactive residues hydrophobically interacted with the catalytic (Ser630) or substrate-binding (Tyr629, Tyr547, Tyr666 and Phe357) hotspots of DPPIV. Molecular docking prediction also suggested the presence of secondary hotspots (Arg125, His126, Gly355, Pro359, Ile405, Asp545, Val546, Cys551, Cys552, Gln553, Trp627, Tyr662, Ala707, Asp709, Glu738, Asp739, Gly741, Ile742 and Tyr752) to support peptide binding. In conclusion, outcome of the current review could inspire the design of potent DPPIV inhibitory peptides where the preference for hydrophobic and aliphatic reactive amino acids could be translated into candidate DPPIV-targeting sequences given their ability to engage with DPPIV hotspots.http://www.sciencedirect.com/science/article/pii/S2772753X23000643Anti-diabetesBioactive peptideDPPIV hotspotsDPPIV inhibitorMolecular dockingStructure-activity relationship |
| spellingShingle | Ainolsyakira Mohd Rodhi Pei-Gee Yap Olalere Olusegun Abayomi Chee-Yuen Gan A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis Food Chemistry Advances Anti-diabetes Bioactive peptide DPPIV hotspots DPPIV inhibitor Molecular docking Structure-activity relationship |
| title | A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis |
| title_full | A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis |
| title_fullStr | A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis |
| title_full_unstemmed | A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis |
| title_short | A review on the types of amino acid at ultimate, penultimate and antepenultimate position in some dipeptidyl-peptidase IV inhibitory peptides based on molecular docking analysis |
| title_sort | review on the types of amino acid at ultimate penultimate and antepenultimate position in some dipeptidyl peptidase iv inhibitory peptides based on molecular docking analysis |
| topic | Anti-diabetes Bioactive peptide DPPIV hotspots DPPIV inhibitor Molecular docking Structure-activity relationship |
| url | http://www.sciencedirect.com/science/article/pii/S2772753X23000643 |
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