Purification and characterization of the dipeptidyl <scp>peptidase‐IV</scp> inhibitory peptides from eel (<i>Anguilla rostrata</i>) scraps enzymatic hydrolysate for the treatment of type 2 diabetes mellitus

Cao, Hongzhen; Di, Nana; Chen, Jingjing; Zhang, Tao

doi:10.1002/jsfa.12462

Cited by 2 publications

(1 citation statement)

References 34 publications

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“…Notably, no residues binding to KPAGN were found in the active pocket of DPP‐IV. Peptides were able to induce DPP‐IV inactivation through a mixed inhibition mode, which involved the formation of hydrophobic interactions and hydrogen bonds both inside and outside the active site (Cao et al., 2023). KPAGN exerted its inhibitory effect on DPP‐IV by interacting with amino acid residues.…”

Section: Resultsmentioning

confidence: 99%

Two novel angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibiting peptides from tilapia (Oreochromis mossambicus) skin and their molecular docking mechanism

Chen,

Ji,

Luo

et al. 2024

Journal of Food Science

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In the study, papain was used to hydrolyze tilapia (Oreochromis mossambicus) skin to obtain a tilapia skin hydrolysate (TSH) with dual angiotensin‐converting enzyme (ACE) and dipeptidyl peptidase IV (DPP‐IV) inhibitory activities. The resulting TSH was sequentially fractionated by ultrafiltration, size exclusion separation chromatography, and reverse‐phase high‐performance liquid chromatography. Its inhibitory effects on ACE and DPP‐IV were determined by commercial reagent kits. Two peptides purified from TSH were identified as Gly‐Pro‐Leu‐Gly‐Ala‐Leu (GPLGAL) and Lys‐Pro‐Ala‐Gly‐Asn (KPAGN) by the ultra‐performance liquid chromatography–tandem mass spectrometry (UPLC–MS/MS). Inhibitory concentration (IC50) of GPLGAL on ACE and DPP‐IV were 117.20 ± 1.69 and 187.10 ± 2.75 µM, respectively. IC50 of KPAGN on ACE and DPP‐IV were 137.40 ± 2.33 and 259.20 ± 2.85 µM, respectively. The molecular simulation demonstrated that the binding affinities of GPLGAL to ACE and DPP‐IV proteins were −8.5 and −7.4 kcal/mol, respectively, whereas those of KPAGN to ACE and DPP‐IV proteins were −7.9 and −6.7 kcal/mol, respectively. GPLGAL interacted with 21 amino acid residues of the ACE active site, whereas KPAGN engaged with 19 amino acid residues. Additionally, GPLGAL interacted with 10 amino acid residues of the DPP‐IV active site, whereas KPAGN engaged with 13 amino acid residues. The two peptides predominantly occupied the active sites of ACE (His513, Tyr523, and Ala354) and DPP‐IV (Tyr662 and Arg125) through hydrogen bonding. This leads to the deactivation of ACE and DPP‐IV.Practical ApplicationAccelerate tilapia skin development and high‐value utilization; provide foundation for preparing the peptides with dual ACE and DPP‐IV inhibiting activity.

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Section: Resultsmentioning

confidence: 99%