Identification of in vitro angiotensin‐converting enzyme and dipeptidyl peptidase IV inhibitory peptides from draft beer by virtual screening and molecular docking

Abstract

BACKGROUND: Hypertension and diabetes are two kinds of senile diseases which often occur simultaneously. The commonly used drugs in clinic may produce certain side effects. Food-derived polypeptide is a kind of polypeptide with great development potential, which has many functions of regulating human physiological function. Beer is rich in nutrition but there are few researches on bioactive peptides in beer.RESULTS: In this study, a rapid virtual screening method was established to obtain bioactive peptides from Tsingtao draft beer. The peptide sequence was analyzed by ultra-performance liquid chromatography-quadrupole-Orbitrap-tandem mass spectrometry (UPLC-Q-Orbitrap-MS 2 ), and 50 peptides were identified. Eight peptides with potential biological activities were screened by using Peptide Ranker software and previous literature references. On the basis of absorption prediction, toxicity prediction, and molecular docking analysis, LNFDPNR and LPQQQAQFK were finally confirmed. The molecular docking results showed that two peptides could bind angiotensin-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) tightly by hydrogen bonding and hydrophobic interaction. The in vitro activity evaluation results showed that two peptides had obvious ACE and DPP-IV inhibitory activity.CONCLUSION: This study established a method for rapidly screening bioactive peptides from Tsingtao draft beer, screened two ACE and DPP-IV inhibitory peptides in beer and analyzed their active action mechanism. This article may have great theoretical significance and practical value to further explore the health function of beer.

Identification of Novel Umami Peptides in Termitornyces albuminosus (Berk) Heim Soup by In Silico Analyses Combined with Sensory Evaluation: Discovering Potential Mechanism of Umami Taste Formation with Molecular Perspective

“…The gradient was set as follows: 0–3 min, 5.0% B; 3–10 min, 5.0–10.0% B; 10–15 min, 10–20.0% B; 15–20 min, 20–95% B; 20–22 min, 95–5.0% B; 22–25 min, 5.0% B. Other mass parameters were set with reference to a previous study . Peaks Studio 8.0 software (Bioinformatics Solutions, Inc., Waterloo, ON, Canada) was used to analyze and process the MS data.…”

Natural products from plants targeting key enzymes for the future development of antidiabetic agents

“…Emodin (82), an anthraquinone, rosmarinic acid (99), a phenylpropanoid, and some stilbenoids are among the most active polyphenols; some of these compounds have shown antidiabetic effects in vivo and in vitro targeting other enzymes and receptors involved in glucose metabolism.…”

“…In this review, we will focus only on those peptides originating from vegetal dietary proteins, which according to a few investigations, can inhibit DPP-IV in vitro. [78][79][80][81] The most active peptides found in this review are summarized in Table 2, [82][83][84][85][86][87][88][89][90][91] which includes amino acid sequences, inhibitory activities, positive controls, and natural sources.…”

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

“…35 Several studies have demonstrated that DPP-IV is highly specific for Pro residues at the P1 position (the second amino acid residue in NH 2 terminal of peptide) and will preferentially cleave dipeptides containing alanine (Xaa-Ala; where Xaa is any amino acid) or proline (Xaa-Pro) from the N terminus of the peptide. 7 Dipeptidyl peptidase-IV also has a cleavage ability for peptides containing Ser, Gly, and Val at this position. 36,37 Although longer peptide sequence lengths have been reported to increase the inhibitory activity of DPP-IV, the IC 50 values of PGVGGPLGPIGPCYE 22 and TQMVDEEIIMEKFR 10 were 116.1 μM and 63.14 μM, respectively.…”

“…6 However, several adverse drug reactions, such as headaches, infection of the upper respiratory tract, and vascular problems, have been identified in patient populations administered these drugs on a long-term basis. 7 Although not as effective as synthetic drugs, the bioactive peptides released from food proteins could cause fewer undesirable side effects. 8 The search for fresh, efficient, and safe DPP-IV inhibitors to replace these synthetic drugs has therefore garnered increased interest.…”