Discovery, synthesis, and in vitro evaluation of a novel bioactive peptide for ACE and DPP-IV inhibitory activity
| Autor: | Arpitha Ashok, H. S. Aparna, N. Brijesha |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Dipeptidyl Peptidase 4
Peptidyl-Dipeptidase A 01 natural sciences Hydrolysate 03 medical and health sciences Hydrolysis Structure-Activity Relationship Drug Discovery Humans IC50 030304 developmental biology Pharmacology chemistry.chemical_classification 0303 health sciences biology Dose-Response Relationship Drug Molecular Structure 010405 organic chemistry Organic Chemistry Angiotensin-converting enzyme Biological activity General Medicine In vitro 0104 chemical sciences Amino acid Biochemistry chemistry Membrane protein biology.protein Peptides |
| Zdroj: | European journal of medicinal chemistry. 180 |
| ISSN: | 1768-3254 |
| Popis: | Biologically active or bioactive peptides are unique amino acid sequences found encrypted in food proteins. These peptides, upon hydrolysis, can exert positive physiological effects on human health, different from that of their native protein. These effects are brought about by their interaction with specific targets in the body, thereby, mimicking physiologically relevant peptides. Peptides are derived from food proteins, they are popular natural alternatives for the management of common metabolic disorders. In the present study, we aimed to identify bioactive peptide sequences (less than 3 kDa) from fat globule membrane protein (FGMP) hydrolysates of buffalo colostrum using a combination of empirical, computational and in vitro methods. The empirical approach aided in the identification of 89 FGMP peptides (m/z-415 to 2939) which were annotated and profiled for bioactivity. Few lead peptides were analyzed by molecular docking for the inhibitory potential of Angiotensin Converting Enzyme (ACE) and Dipeptidyl Peptidase-IV (DPP-IV). A heptapeptide (m/z-723.3) synthesized was found to inhibit ACE (IC50: 74.27 μM) and DPP-IV (IC50: 3.83 mM). |
| Databáze: | OpenAIRE |
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