دورية أكاديمية
Identification of DPP-IV inhibitory peptides derived from buffalo colostrum: Mining through bioinformatics, in silico and in vitro approaches.
| العنوان: | Identification of DPP-IV inhibitory peptides derived from buffalo colostrum: Mining through bioinformatics, in silico and in vitro approaches. |
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| المؤلفون: | Ashok A; DOS in Biotechnology, University of Mysore, Mysuru, India., H S A; DOS in Biotechnology, University of Mysore, Mysuru, India. |
| المصدر: | Journal of molecular recognition : JMR [J Mol Recognit] 2024 Jul; Vol. 37 (4), pp. e3090. Date of Electronic Publication: 2024 May 27. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: John Wiley & Sons Country of Publication: England NLM ID: 9004580 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1099-1352 (Electronic) Linking ISSN: 09523499 NLM ISO Abbreviation: J Mol Recognit Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Original Publication: London, UK : Heydon & Son, c1988- |
| مواضيع طبية MeSH: | Buffaloes* , Colostrum*/chemistry , Dipeptidyl-Peptidase IV Inhibitors*/chemistry , Dipeptidyl-Peptidase IV Inhibitors*/pharmacology , Dipeptidyl Peptidase 4*/chemistry , Dipeptidyl Peptidase 4*/metabolism , Molecular Docking Simulation* , Computational Biology* , Peptides*/chemistry , Peptides*/pharmacology, Animals ; Prolyl Oligopeptidases/metabolism ; Prolyl Oligopeptidases/chemistry ; Humans ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/metabolism ; Amino Acid Sequence ; Computer Simulation ; Female |
| مستخلص: | Bioactive peptides derived from foods provide physiological health benefits beyond nutrition. This study focused on profiling small peptide inhibitors against two key serine proteases, dipeptidyl peptidase-IV (DPP-IV) and prolyl oligopeptidase (POP). DPP-IV is a well-known protein involved in diverse pathways regulating inflammation, renal, cardiovascular physiology, and glucose homeostasis. POP is yet another key target protein for neurodegenerative disorders. The study evaluated peptide libraries of buffalo colostrum whey and fat globule membrane proteins derived from pepsin and pepsin-pancreatin digestion through in silico web tools and structure-based analysis by molecular docking and binding free-energy estimation, followed by in vitro assay for DPP-IV inhibition for the lead peptides. The bioinformatic study indicated 49 peptides presented motifs with DPP-IV inhibition while 5 peptides with sequences for POP inhibition. In the molecular docking interactions study, 22 peptides interacted with active site residues of DPP-IV and 3 peptides with that of POP. The synthesized peptides, SFVSEVPEL and LTFQHNF inhibited DPP-IV in vitro with an IC50 of 193.5 μM and 1.782 mM, respectively. The study revealed the key residues for inhibition of DPP-IV and POP thus affirming the DPP-IV inhibitory potential of milk-derived peptides. (© 2024 John Wiley & Sons Ltd.) |
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| معلومات مُعتمدة: | Karnataka Science and Technology Promotion Society; Indian Council of Medical Research; Science and Engineering Research Board |
| فهرسة مساهمة: | Keywords: DPP‐IV; bioactive peptides; diabetes; dipeptidyl peptidase; milk peptides |
| المشرفين على المادة: | 0 (Dipeptidyl-Peptidase IV Inhibitors) EC 3.4.14.5 (Dipeptidyl Peptidase 4) 0 (Peptides) EC 3.4.21.26 (Prolyl Oligopeptidases) EC 3.4.21.- (Serine Endopeptidases) |
| تواريخ الأحداث: | Date Created: 20240528 Date Completed: 20240618 Latest Revision: 20240618 |
| رمز التحديث: | 20240619 |
| DOI: | 10.1002/jmr.3090 |
| PMID: | 38803118 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1099-1352 |
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| DOI: | 10.1002/jmr.3090 |