The biological role of prolyl oligopeptidase and the procognitive potential of its peptidic inhibitors from food proteins

Taraszkiewicz, Antoni; Sinkiewicz, Izabela; Sommer, Agata; Staroszczyk, Hanna

doi:10.1080/10408398.2023.2170973

Cited by 5 publications

(3 citation statements)

References 141 publications

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“…The results suggest that the DH may be important in obtaining potent PEP inhibitory peptides. The importance of the DH on the inhibitory activity has also been reported by Taraszkiewicz et al [38], who found that most PEP inhibitory peptides have a short length and low molecular weight. Lajmi et al [41] also observed the importance of low-molecular-weight peptides in the PEP inhibitory activity of protein hydrolysates.…”

Section: Pep Inhibitory Activitysupporting

confidence: 62%

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Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

Bougatef,

Sila,

Bougatef

et al. 2024

Marine Drugs

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The industrial processing of Argentine shortfin squid to obtain rings generates a significant amount of protein-rich waste, including the skin, which is rich in collagen and attached myofibrillar proteins. This waste is generally discarded. In this study, skin was used as a source of proteins that were hydrolysed using Trypsin, Esperase® or Alcalase®, which released peptides with antioxidant potential and, in particular, antihypertensive (ACE inhibition), hypoglycemic (DPP-IV inhibition) and/or nootropic (PEP inhibition) potential. Among the three enzymes tested, Esperase® and Alcalase produced hydrolysates with potent ACE-, DPP-IV- and PEP-inhibiting properties. These hydrolysates underwent chromatography fractionation, and the composition of the most bioactive fractions was analysed using HPLC-MS-MS. The fractions with the highest bioactivity exhibited very low IC50 values (16 and 66 µg/mL for ACE inhibition, 97 µg/mL for DPP-IV inhibition and 55 µg/mL for PEP inhibition) and were mainly derived from the hydrolysate obtained using Esperase®. The presence of Leu at the C-terminal appeared to be crucial for the ACE inhibitory activity of these fractions. The DPP-IV inhibitory activity of peptides seemed to be determined by the presence of Pro or Ala in the second position from the N-terminus, and Gly and/or Pro in the last C-terminal positions. Similarly, the presence of Pro in the peptides present in the best PEP inhibitory fraction seemed to be important in the inhibitory effect. These results demonstrate that the skin of the Argentine shortfin squid is a valuable source of bioactive peptides, suitable for incorporation into human nutrition as nutraceuticals and food supplements.

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Section: Pep Inhibitory Activitysupporting

confidence: 62%

“…The inhibition of PEP has been considered as a potential treatment for neurodegenerative disorders. In vivo experiments have demonstrated antiamnesic effects of PEP inhibitors in rats [38]. Most PEP inhibitors described in the literature are compounds with a pyrrolidine or a pyrrolidine ring substituted at the P1 site [39].…”

Section: Pep Inhibitory Activitymentioning

confidence: 99%

Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

Bougatef,

Sila,

Bougatef

et al. 2024

Marine Drugs

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“…7,39,40 This surface loop system is an ideal target for inhibitors as it has significant control over the enzyme's catalytic activity as seen in the case of Berberine derivatives. 41 Although there are reports of POP inhibitors derived from milk proteins and peptides as reviewed recently by Taraszkiewicz and colleagues, 42 none of these studies focused on the in silico interactions important for inhibition of POP by the peptide(s). The peptides in the study were found to interact with the residues Trp 595 and Arg 643.…”

Section: Discussionmentioning

confidence: 99%

Identification of DPP‐IV inhibitory peptides derived from buffalo colostrum: Mining through bioinformatics, in silico and in vitro approaches

Ashok,

H. S.

2024

J of Molecular Recognition

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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.

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Efficient degradation of soybean protein B3 subunit in soy sauce by ultrasound-assisted prolyl endopeptidase and its primary mechanism

et al. 2023

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The biological role of prolyl oligopeptidase and the procognitive potential of its peptidic inhibitors from food proteins

Cited by 5 publications

References 141 publications

Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

Protein Hydrolysis as a Way to Valorise Squid-Processing Byproducts: Obtaining and Identification of ACE, DPP-IV and PEP Inhibitory Peptides

Identification of DPP‐IV inhibitory peptides derived from buffalo colostrum: Mining through bioinformatics, in silico and in vitro approaches

Efficient degradation of soybean protein B3 subunit in soy sauce by ultrasound-assisted prolyl endopeptidase and its primary mechanism

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