Preparation, structural properties, and <i>in vitro</i> and <i>in vivo</i> activities of peptides against dipeptidyl peptidase IV (DPP-IV) and α-glucosidase: a general review

Mu, Xijin; Wang, Rongchun; Cheng, Cuilin; Ma, Ying; Zhang, Yingchun; Lu, Weihong

doi:10.1080/10408398.2023.2217444

Cited by 16 publications

(12 citation statements)

References 114 publications

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“…The possible reason was the fifth amino acid of the decapeptide was a Pro residue, which induced a tight turn into the polypeptide chain, leading to the changed conformation of the peptide backbone . A review summarized the published DPP-IV-inhibiting peptides, and there was no link between the length of the peptides and their inhibitory effects . Undeniably, this conclusion was obtained through statistical data, and the influence of other properties (except for peptide length) on the activity could not be completely excluded.…”

Section: Resultsmentioning

confidence: 99%

“…It was reported that the presence of a hydrophobic N-terminal amino acid rather than the overall hydrophobicity of the peptide might be linked to DPP-IV inhibitory properties . Mu et al also reported that amino acids were distributed differently at the fourth (N4) and fifth (N5) positions of the N-terminal for peptides with high inhibitory activity . We also observed that the amino acids at different positions of the peptide had distinct interactions with DPP-IV.…”

Section: Resultsmentioning

confidence: 99%

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Molecular Mechanistic Insights into Dipeptidyl Peptidase-IV Inhibitory Peptides to Decipher the Structural Basis of Activity

Wang,

Zheng,

Udenigwe

et al. 2024

J. Agric. Food Chem.

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Dipeptidyl peptidase-IV (DPP-IV) inhibiting peptides have attracted increased attention because of their possible beneficial effects on glycemic homeostasis. However, the structural basis underpinning their activities has not been well understood. This study combined computational and in vitro investigations to explore the structural basis of DPP-IV inhibitory peptides. We first superimposed the Xaa−Pro-type peptide-like structures from several crystal structures of DPP-IV ligand−protein complexes to analyze the recognition interactions of DPP-IV to peptides. Thereafter, a small set of Xaa−Pro-type peptides was designed to explore the effect of key interactions on inhibitory activity. The intramolecular interaction of Xaa−Pro-type peptides at the first and third positions from the N-terminus was pivotal to their inhibitory activities. Residue interactions between DPP-IV and residues of the peptides at the fourth and fifth positions of the N-terminus contributed significantly to the inhibitory effect of Xaa−Pro-type tetrapeptides and pentapeptides. Based on the interaction descriptors, quantitative structure−activity relationship (QSAR) studies with the DPP-IV inhibitory peptides resulted in valid models with high R 2 values (0.90 for tripeptides; 0.91 for tetrapeptides and pentapeptides) and Q 2 values (0.33 for tripeptides; 0.68 for tetrapeptides and pentapeptides). Taken together, the structural information on DPP-IV and peptides in this study facilitated the development of novel DPP-IV inhibitory peptides.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Molecular Mechanistic Insights into Dipeptidyl Peptidase-IV Inhibitory Peptides to Decipher the Structural Basis of Activity

Wang,

Zheng,

Udenigwe

et al. 2024

J. Agric. Food Chem.

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“…Amino acids with a molecular weight below 3 kDa—including proline, phenylalanine, leucine, and glycine—exhibited sharp α-amylase inhibition, possibly due to the inhibitory effects of these specific amino acid residues. Additionally, Mu et al (2023) emphasized that peptides containing two to eight amino acid compounds, particularly those with more amino acids that are hydrophobic such as proline and leucine, demonstrated increased inhibitory effects on α-glucosidase.…”

Section: Resultsmentioning

confidence: 99%

Peptidomics-based identification of antihypertensive and antidiabetic peptides from sheep milk fermented using Limosilactobacillus fermentum KGL4 MTCC 25515 with anti-inflammatory activity: in silico, in vitro, and molecular docking studies

Pipaliya,

Basaiawmoit,

Sakure

et al. 2024

Front. Chem.

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This study investigated the synthesis of bioactive peptides from sheep milk through fermentation with Limosilactobacillus fermentum KGL4 MTCC 25515 strain and assessed lipase inhibition, ACE inhibition, α-glucosidase inhibition, and α-amylase inhibition activities during the fermentation process. The study observed the highest activities, reaching 74.82%, 70.02%, 72.19%, and 67.08% (lipase inhibition, ACE inhibition, α-glucosidase inhibition, and α-amylase inhibition) after 48 h at 37°C, respectively. Growth optimization experiments revealed that a 2.5% inoculation rate after 48 h of fermentation time resulted in the highest proteolytic activity at 9.88 mg/mL. Additionally, fractions with less than 3 kDa of molecular weight exhibited superior ACE-inhibition and anti-diabetic activities compared to other fractions. Fermentation of sheep milk with KGL4 led to a significant reduction in the excessive production of NO, TNF-α, IL-6, and IL-1β produced in RAW 267.4 cells upon treatment with LPS. Peptides were purified utilizing SDS-PAGE and electrophoresis on 2D gels, identifying a maximum number of proteins bands ranging 10–70 kDa. Peptide sequences were cross-referenced with AHTPDB and BIOPEP databases, confirming potential antihypertensive and antidiabetic properties. Notably, the peptide (GPFPILV) exhibited the highest HPEPDOCK score against both α-amylase and ACE.

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“…DPP-IV inhibitory peptides can exert their inhibitory effect via different mechanisms depending on their ability to bind to different domains of the enzyme. Nong and Hsu [36] and Mu et al [56] suggested that the presence of certain residues in the N-terminal position is important for DPP-IV inhibition. Specifically, Gly, Ala, Pro, Ile, Leu, Met, Val or Glu residues interact with the hydrophobic pocket of the active site.…”

Section: Identification Of the Peptide Composition Of The Most Potent...mentioning

confidence: 99%

“…Peptides with glycine in this position were particularly relevant (Table 7). The presence of proline or alanine at the second N-terminal position favors DPP-IV inhibition due to the affinity of the enzyme for these ligands [56]. In the fraction, it was observed in about 30% of the peptides, for example in GADGERGPRGNRGDTGAS, GPAGP(+15.99)P(+15.99)GAPG or GPTGP(+15.99)AGPAG (Table 7).…”

Section: Identification Of the Peptide Composition Of The Most Potent...mentioning

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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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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Preparation, structural properties, and in vitro and in vivo activities of peptides against dipeptidyl peptidase IV (DPP-IV) and α-glucosidase: a general review

Cited by 16 publications

References 114 publications

Molecular Mechanistic Insights into Dipeptidyl Peptidase-IV Inhibitory Peptides to Decipher the Structural Basis of Activity

Molecular Mechanistic Insights into Dipeptidyl Peptidase-IV Inhibitory Peptides to Decipher the Structural Basis of Activity

Peptidomics-based identification of antihypertensive and antidiabetic peptides from sheep milk fermented using Limosilactobacillus fermentum KGL4 MTCC 25515 with anti-inflammatory activity: in silico, in vitro, and molecular docking studies

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

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