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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sila, Assaad Alvarez, Oscar Martinez Haddar, Anissa Frikha, Fakher Dhulster, Pascal Nedjar-Arroume, Naima Bougatef, Ali |
| Description | Country affiliation: France Author Affiliation: Sila A ( Unité Enzyme et Bioconversion, Ecole Nationale d'Ingénieurs de Sfax, B.P '1173',3038 Sfax, Tunisia); Alvarez OM ( Institute of Food Science, Technology and Nutrition (ICTAN-CSIC), Madrid, Spain.); Haddar A ( Unité Enzyme et Bioconversion, Ecole Nationale d'Ingénieurs de Sfax, B.P '1173',3038 Sfax, Tunisia.); Frikha F ( Faculty of Science of Sfax, Route Soukra km 3.5, Sfax, Tunisia.); Dhulster P ( Institut Charles Viollette, équipe ProBioGEM, Polytech'Lille, 59655 Villeneuve d'Ascq Cedex, France.); Nedjar-Arroume N ( Institut Charles Viollette, équipe ProBioGEM, Polytech'Lille, 59655 Villeneuve d'Ascq Cedex, France.); Bougatef A ( Unité Enzyme et Bioconversion, Ecole Nationale d'Ingénieurs de Sfax, B.P '1173',3038 Sfax, Tunisia. Electronic address: ali.bougatef79@gmail.com.) |
| Abstract | Inhibition of DPP-IV may improve glycemic control in diabetics by preventing the rapid breakdown and there by prolonging the physiological action of incretin hormones. Barbel muscle protein hydrolysate (BMPH) was noted to exhibit DPP-IV inhibitory activity, with an IC50 value of 1.94mg/mL. It was fractionated into five major fractions (FI-FV) by size exclusion chromatography using a Superdex peptide. The FIII fraction was noted to display the highest inhibitory activity, with an IC50 value of 1.23mg/mL, and was, therefore, further fractionated by RP-HPLC. Four major peptide sub-fractions were selected. The results revealed that the SF4 sub-fraction showed the highest DPP-IV inhibitory activity, with an IC50 value of 0.21mg/mL. This sub-fraction was submitted to RP-HPLC, ESI-MS, and ESI-MS/MS analyses. The findings indicated that SF4 consisted of two peptides (IC50=96µg/mL), namely PP1 and PP2, whose structures were identified as Trp-Ser-Gly (330Da) and Phe-Ser-Asp (349Da), respectively. This is the first report of these sequences from barbel proteins. The structural modelling through docking simulations results with DPP-IV showed that the Trp-Ser-Gly peptide bound to DPP-IV with high affinity. Overall, the results suggested that BMPH can be considered as a promising natural source of DPP-IV inhibitory peptides. |
| File Format | HTM / HTML |
| ISSN | 15700232 |
| Volume Number | 1008 |
| e-ISSN | 1873376X |
| Journal | Journal of Chromatography B |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-01-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Analytical Chemistry Dipeptidyl-peptidase Iv Inhibitors Chemistry Peptides Chromatography, High Pressure Liquid Chromatography, Reverse-phase Hydrolysis Models, Molecular Protein Conformation Spectrometry, Mass, Electrospray Ionization Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine Analytical Chemistry Clinical Biochemistry Biochemistry |
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