Characterisation of the potential of β-lactoglobulin and α-lactalbumin as sources of bioactive peptides affecting incretin function: In silico and in vitro comparative studies

2015 ◽  
Vol 48 ◽  
pp. 66-72 ◽  
Author(s):  
Giovanni Tulipano ◽  
Lara Faggi ◽  
Alessandro Nardone ◽  
Daniela Cocchi ◽  
Anna Maria Caroli
Keyword(s):  
Comparative Studies ◽  
In Silico ◽  
Bioactive Peptides ◽  
Β Lactoglobulin

In vitro digestibility of bioactive peptides derived from bovine β-lactoglobulin

2006 ◽  
Vol 16 (4) ◽  
pp. 294-302 ◽  
Author(s):  
Samira Roufik ◽  
Sylvie F. Gauthier ◽  
Sylvie L. Turgeon
Keyword(s):  
Bioactive Peptides ◽  
In Vitro Digestibility ◽  
Β Lactoglobulin

scholarly journals In Silico and In Vitro Assessment of Portuguese Oyster (Crassostrea angulata) Proteins as Precursor of Bioactive Peptides

2019 ◽  
Vol 20 (20) ◽  
pp. 5191 ◽  
Author(s):  
Honey Lyn R. Gomez ◽  
Jose P. Peralta ◽  
Lhumen A. Tejano ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
In Silico Analysis ◽  
In Vitro Tests ◽  
Dpp Iv ◽  
Crassostrea Angulata ◽  
Vitro Analysis

In this study, the potential bioactivities of Portuguese oyster (Crassostrea angulata) proteins were predicted through in silico analyses and confirmed by in vitro tests. C. angulata proteins were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by proteomics techniques. Hydrolysis simulation by BIOPEP-UWM database revealed that pepsin (pH > 2) can theoretically release greatest amount of bioactive peptides from C. angulata proteins, predominantly angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory peptides, followed by stem bromelain and papain. Hydrolysates produced by pepsin, bromelain and papain have shown ACE and DPP-IV inhibitory activities in vitro, with pepsin hydrolysate (PEH) having the strongest activity of 78.18% and 44.34% at 2 mg/mL, respectively. Bioactivity assays of PEH fractions showed that low molecular weight (MW) fractions possessed stronger inhibitory activity than crude hydrolysate. Overall, in vitro analysis results corresponded with in silico predictions. Current findings suggest that in silico analysis is a rapid method to predict bioactive peptides in food proteins and determine suitable enzymes for hydrolysis. Moreover, C. angulata proteins can be a potential source of peptides with pharmaceutical and nutraceutical application.

scholarly journals Therapeutic Potential of Tuna Backbone Peptide and Its Analogs: An In Vitro and In Silico Study

Molecules ◽  
2021 ◽  
Vol 26 (7) ◽  
pp. 2064
Author(s):  
Varun Gopinatth ◽  
Rufa L. Mendez ◽  
Elaine Ballinger ◽  
Jung Yeon Kwon
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Therapeutic Potential ◽  
Antioxidant Activities ◽  
Radical Scavenging ◽  
Activity Assay ◽  
In Silico Study ◽  
The Impact ◽  
Potent Inhibitory Activity

Tuna backbone peptide (TBP) has been reported to exert potent inhibitory activity against lipid peroxidation in vitro. Since this bears relevant physiological implications, this study was undertaken to assess the impact of peptide modifications on its bioactivity and other therapeutic potential using in vitro and in silico approach. Some TBP analogs, despite lower purity than the parent peptide, exerted promising antioxidant activities in vitro demonstrated by ABTS radical scavenging assay and cellular antioxidant activity assay. In silico digestion of the peptides resulted in the generation of antioxidant, angiotensin-converting enzyme (ACE), and dipeptidyl peptidase-IV (DPPIV) inhibitory dipeptides. Using bioinformatics platforms, we found five stable TBP analogs that hold therapeutic potential with their predicted multifunctionality, stability, non-toxicity, and low bitterness intensity. This work shows how screening and prospecting for bioactive peptides can be improved with the use of in vitro and in silico approaches.

scholarly journals Bioactive peptides from beef products fermented by acid whey – in vitro and in silico study

2019 ◽  
Vol 76 (4) ◽  
pp. 311-320 ◽  
Author(s):  
Paulina Kęska ◽  
Karolina Maria Wójciak ◽  
Joanna Stadnik
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
In Silico Study ◽  
Beef Products ◽  
Acid Whey

scholarly journals Pacific Dulse Protein: A Promising Source of Bioactive Peptides

2021 ◽  
Vol 5 (Supplement_2) ◽  
pp. 597-597
Author(s):  
Rufa Mendez ◽  
Jung Kwon
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
De Novo ◽  
De Novo Sequencing ◽  
Metabolic Effects ◽  
Health Improvement ◽  
Predictive Values ◽  
Anti Inflammatory ◽  
Promising Source

Abstract Objectives Pacific dulse (Devaleraea mollis) is a protein-rich seaweed in the Pacific Northwest and increasingly being cultivated as food resource. Our previous work showed that dietary supplementation of dulse exerted beneficial metabolic effects to the high-fat fed mouse model. This study aims to evaluate the potential of the seaweed protein from dulse as a precursor for bioactive peptide (BAP) generation. Methods The potential of Pacific dulse protein as BAP precursor was assessed using in vitro and in silico approaches. Hydrolysates were prepared from the hydrated freeze-dried protein isolates which were digested using commercial proteases. These were used for the in vitro screening for antioxidant and anti-inflammatory activities as well as the inhibition of Angiotensin-converting enzyme 1 (ACE-1), Renin, and Dipeptidyl peptidase IV (DPPIV). Peptides in the hydrolysates that exhibit the highest activities were identified using de novo sequencing. Identified peptides were shortlisted based on their potential to be bioactive using Peptide Ranker and specific bioactivity scores were obtained using in silico platforms such as iDPPIV-SCM and PreAIP. To determine whether the consumption of the seaweed protein may help give rise to some bioactive peptides, annotated protein sequences of the seaweed material were obtained from UniProtKB and were subjected to in silico digestion using pepsin, chymotrypsin, and trypsin through BIOPEP. Bioactivity indices of the generated peptide fragments were recorded as predictive values. Results In silico digestion showed that dulse proteins can give rise to ACE-1, DPP-IV, and renin inhibitors, as well as antioxidant peptides. Hydrolysates exerted inhibitory effects on human ACE-1, DPPIV, and renin in vitro. ABTS radical scavenging assay and cellular antioxidant activity assay in human hepatocytes indicated the strong antioxidant potential of dulse BAP. Peptides identified through de novo sequencing had high predictive scores for DDPIV inhibition and anti-inflammatory potential. Conclusions Pacific dulse proteins is a promising precursor for the generation of BAPs that may exert beneficial health activities and support metabolic health improvement. Funding Sources Oregon State University Agricultural Research Foundation.

Prediction of Bioactive Peptides From Chicken Feather and Pig Hair Keratins Using In Silico Analysis Based on Fragmentomic Approach

2022 ◽  
Vol 28 ◽  
Author(s):  
Antoni Taraszkiewicz ◽  
Izabela Sinkiewicz ◽  
Agata Sommer ◽  
Małgorzata Dąbrowska ◽  
Hanna Staroszczyk
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
In Silico Analysis ◽  
In Vivo Studies ◽  
Animal Origin ◽  
Waste Products ◽  
Theoretical Predictions ◽  
Keratin Hydrolysis

Background: Keratin is among the most abundant structural proteins of animal origin, however it remains broadly underutilized. Objective: Bioinformatic investigation was performed to evaluate selected keratins originating from mass-produced waste products, i.e., chicken feathers and pig hair, as potential sources of bioactive peptides. Methods: Pepsin, trypsin, chymotrypsin, papain, and subtilisin were used for in silico keratinolysis with the use of “Enzyme(s) action” and fragmentomic analysis of theoretical products was performed using “Profiles of potential biological activity” in BIOPEP-UWM database of bioactive peptides. Bioactivity probability calculation and toxicity prediction of the peptides obtained were estimated using PeptideRanker and ToxinPred tools, respectively. Results: Our results showed that the keratins are a potential source of a variety of biopeptides, including dipeptidyl peptidase IV, angiotensin converting enzyme, prolyl endopeptidase inhibitory and antioxidative. Papain and subtilisin were found to be the most appropriate enzymes for keratin hydrolysis. This study presents possible structures of keratin-derived bioactive peptides that have not been previously described. Conclusion: Our data suggest additional in vitro and in vivo studies to verify theoretical predictions and further investigate the possibility of using keratin-rich waste as a source of peptide nutraceuticals.

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