scholarly journals Prediction of Bioactive Peptides from Chlorella sorokiniana Proteins Using Proteomic Techniques in Combination with Bioinformatics Analyses

2019 ◽  
Vol 20 (7) ◽  
pp. 1786 ◽  
Author(s):  
Lhumen A. Tejano ◽  
Jose P. Peralta ◽  
Encarnacion Emilia S. Yap ◽  
Fenny Crista A. Panjaitan ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Biological Activities ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
In Silico Analysis ◽  
Chlorella Sorokiniana ◽  
Molecular Characteristics ◽  
Sds Page ◽  
Silico Analysis

Chlorella is one of the most nutritionally important microalgae with high protein content and can be a good source of potential bioactive peptides. In the current study, isolated proteins from Chlorella sorokiniana were subjected to in silico analysis to predict potential peptides with biological activities. Molecular characteristics of proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and proteomics techniques. A total of eight proteins were identified by proteomics techniques from 10 protein bands of the SDS-PAGE. The predictive result by BIOPEP’s profile of bioactive peptides tools suggested that proteins of C. sorokiniana have the highest number of dipeptidyl peptidase-IV (DPP IV) inhibitors, with high occurrence of other bioactive peptides such as angiotensin-I converting enzyme (ACE) inhibitor, glucose uptake stimulant, antioxidant, regulating, anti-amnestic and antithrombotic peptides. In silico analysis of enzymatic hydrolysis revealed that pepsin (pH > 2), bromelain and papain were proteases that can release relatively larger quantity of bioactive peptides. In addition, combinations of different enzymes in hydrolysis were observed to dispense higher numbers of bioactive peptides from proteins compared to using individual proteases. Results suggest the potential of protein isolated from C. sorokiniana could be a source of high value products with pharmaceutical and nutraceutical application potential.

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 Potential Biological Activities of Peptides Generated during Casein Proteolysis by Curly Kale (Brassica oleracea L. var. sabellica L.) Leaf Extract: An In Silico Preliminary Study

Foods ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2877
Author(s):  
Magdalena Polak-Berecka ◽  
Magdalena Michalak-Tomczyk ◽  
Katarzyna Skrzypczak ◽  
Katarzyna Michalak ◽  
Kamila Rachwał ◽  
...  
Keyword(s):  
In Silico ◽  
Leaf Extract ◽  
Degradation Products ◽  
Biological Activities ◽  
Protein Profile ◽  
In Silico Analysis ◽  
Amino Acid Sequences ◽  
Casein Hydrolysis ◽  
Sds Page ◽  
Silico Analysis

This study is a brief report on the proteolytic activity of curly kale leaf extract against casein. Casein degradation products and an in silico analysis of the biological activity of the peptides obtained was performed. The efficiency of casein hydrolysis by curly kale extract was determined using SDS–PAGE and by peptide concentration determination. The pattern of the enzymatic activity was determined by MALDI–TOF MS analysis. The results showed that α- and β-casein were more resistant to curly kale extract hydrolysis, whereas κ-casein was absent in the protein profile after 8 h of proteolysis, and all casein fractions were completely hydrolyzed after 24 h of incubation. Based on sequence analysis, seven peptides were identified, with molecular mass in the range of 1151–3024 Da. All the peptides were products of β-casein hydrolysis. The identified amino acid sequences were analyzed in BIOPEP, MBPDB, and FeptideDB databases in order to detect the potential activities of the peptides. In silico analysis suggests that the β-casein-derived peptides possess sequences of peptides with ACE inhibitory, antioxidant, dipeptidyl peptidase IV inhibitory, antithrombotic, immunomodulatory, and antiamnesic bioactivity. Our study was first to evaluate the possibility of applying curly kale leaf extract to generate biopeptides through β-casein hydrolysis.

Majra Honey Abrogated the Normal and Cancer Cells Proliferation Inhibition by Juniperus procera Extract and Extract/Honey Generated AgNPs

2020 ◽  
Vol 20 (8) ◽  
pp. 970-981
Author(s):  
Hamed A. Ghramh ◽  
Essam H. Ibrahim ◽  
Mona Kilnay
Keyword(s):  
Anticancer Activity ◽  
Cancer Cells ◽  
Biological Activities ◽  
Sugar Content ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Bioactive Molecules ◽  
Sds Page ◽  
Splenic Cells ◽  
Juniperus Procera

Background: Juniperus procera and Majra honey are well-known as a folk medicine in many countries. Objectives: This work aimed to study the immunomodulatory effects after mixing Majra honey, J. procera water leaves extract and silver Nanoparticles (AgNPs) on immune or cancer cells. Methods: Juniperus procera water leaves extract and 20% Majra honey were prepared. Both the extract and honey were used separately to synthesize AgNPs. AgNPs were characterized using UV/Vis spectrophotometry and electron microscopy. Bioactive molecules in honey and the extract were explored using Fourier Transform Infrared (FT-IR) spectroscopy. Protein profile of honey was explored using Sodium Dodecyl Sulfate- Polyacrylamide Gel Electrophoresis (SDS-PAGE) and honey sugar content was determined using High- Performance Liquid Chromatography (HPLC). Biological activities of honey and the extract were tested. Results: The results demonstrated the ability of the extract/honey to produce AgNPs in a spherical shape. The extract/honey contained many functional groups. SDS-PAGE of Majra honey showed many protein bands. HPLC revealed honey is of good quality and no external additives are added to it. The extract and extract+ AgNPs inhibited the growth of normal rat splenic cells while honey stimulated it. The extract+honey turned stimulatory to the splenic cells’ growth and significantly diminished the inhibitory potential of the extract containing AgNPs. Both the extract and honey have antimicrobial activities, this potential increased in the presence of AgNPs. Honey and Honey+AgNPs inhibited HepG2 cancer cell proliferation while Hela cell growth inhibited only with honey+AgNPs. Conclusion: Both honey and the extract have antibacterial and immunomodulatory potentials as well as the power to produce AgNPs. Majra honey alone showed anticancer activity against HepGe2 cells, but not against Hela cells, and when contained AgNPs had anticancer activity on both cell lines. Mixing of Majra honey with J. procera extract showed characterized immunomodulatory potentials that can be described as immunostimulant.

scholarly journals In Silico Analysis of Bioactive Peptides Released from Giant Grouper (Epinephelus lanceolatus) Roe Proteins Identified by Proteomics Approach

Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2910 ◽  
Author(s):  
Fenny Panjaitan ◽  
Honey Gomez ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
In Silico Analysis ◽  
Epinephelus Coioides ◽  
Accession Number ◽  
Inhibitory Peptides ◽  
Dpp Iv ◽  
Ncbi Accession ◽  
Silico Analysis ◽  
Ncbi Accession Number

Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were characterized through compiled proteomics techniques (SDS-PAGE, in-gel digestion, mass spectrometry and on-line Mascot database analysis). These proteins were subjected to in silico analysis using BLAST and BIOPEP-UWM database. Sequence similarity search by BLAST revealed that the aligned vitellogenin sequences from Epinephelus coioides and Epinephelus lanceolatus share 70% identity, which indicates that the sequence sample has significant similarity with proteins in sequence databases. Moreover, prediction of potential bioactivities through BIOPEP-UWM database resulted in high numbers of peptides predominantly with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE-I) inhibitory activities. Pepsin (pH > 2) was predicted to be the most promising enzyme for the production of bioactive peptides from GR protein, which theoretically released 82 DPP-IV inhibitory peptides and 47 ACE-I inhibitory peptides. Overall, this work highlighted the potentiality of giant grouper roe as raw material for the generation of pharmaceutical products. Furthermore, the application of proteomics and in silico techniques provided rapid identification of proteins and useful prediction of its potential bioactivities.

Purification of PRL receptors from toad kidney: comparisons with rabbit mammary PRL receptors

1988 ◽  
Vol 254 (3) ◽  
pp. C372-C382 ◽  
Author(s):  
M. Dunand ◽  
J. P. Kraehenbuhl ◽  
B. C. Rossier ◽  
M. L. Aubert
Keyword(s):  
Mammalian Species ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Structural Features ◽  
Polyclonal Antiserum ◽  
Partial Purification ◽  
Molecular Characteristics ◽  
Binding Characteristics ◽  
Sds Page

The binding characteristics of the prolactin (PRL) receptors present in toad (Bufo marinus) kidneys were investigated and compared to those of PRL receptors present in rabbit mammary glands. The molecular characteristics of the Triton X-100 solubilized renal and mammary PRL receptors were assessed by gel filtration and by migration analysis on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) after affinity labeling of the binding sites with 125I-human growth hormone. Similar results were obtained for both receptors. Partial purification of the toad PRL receptor could be achieved by affinity chromatography. The molecular weight of this purified receptor could be determined by analysis on SDS-PAGE. With the use of a polyclonal antiserum raised against a purified preparation of rabbit mammary PRL receptor, one or several antigenic epitope(s) could be identified on the core of the toad renal PRL receptor. In conclusion, although the structure and the biological role(s) of PRL have substantially changed during evolution, the receptor for this hormone has retained many of its structural features as could be assessed between an amphibian and a mammalian species on functionally different target tissues.

In silico analysis of interaction pattern switching in ligand⋯receptor binding in Golgi α-mannosidase II induced by the protonated states of inhibitors

2017 ◽  
Vol 19 (19) ◽  
pp. 12527-12537 ◽  
Author(s):  
V. Sladek ◽  
J. Kóňa ◽  
H. Tokiwa
Keyword(s):  
Receptor Binding ◽  
In Silico ◽  
Active Sites ◽  
Biological Activities ◽  
In Silico Analysis ◽  
Interaction Pattern ◽  
Binding Modes ◽  
Silico Analysis

Different binding modes for charge-neutral and protonated inhibitor forms in Golgi α-mannosidase II active sites may influence their biological activities.

scholarly journals Biological Insights of Fluoroaryl-2,2′-Bichalcophene Compounds on Multi-Drug Resistant Staphylococcus aureus

Molecules ◽  
2020 ◽  
Vol 26 (1) ◽  
pp. 139
Author(s):  
Sally Elmogy ◽  
Mohamed A. Ismail ◽  
Rabeay Y. A. Hassan ◽  
Ahmed Noureldeen ◽  
Hadeer Darwish ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Agents ◽  
Biological Activities ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Ultrastructural Level ◽  
Biofilm Inhibition ◽  
Sds Page ◽  
The Impact

Resistance of bacteria to multiple antibiotics is a significant health problem; hence, to continually respond to this challenge, different antibacterial agents must be constantly discovered. In this work, fluoroaryl-2,2′-bichalcophene derivatives were chemically synthesized and their biological activities were evaluated against Staphylococcus aureus (S. aureus). The impact of the investigated bichalcophene derivatives was studied on the ultrastructural level via scanning electron microscopy (SEM), molecular level via sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) method and on the biofilm inhibition via the electrochemical biosensors. Arylbichalcophenes’ antibacterial activity against S. aureus was affected by the presence and location of fluorine atoms. The fluorobithiophene derivative MA-1156 displayed the best minimum inhibitory concentration (MIC) value of 16 µM among the tested fluoroarylbichalcophenes. Over a period of seven days, S. aureus did not develop any resistance against the tested fluoroarylbichalcophenes at higher concentrations. The impact of fluoroarylbichalcophenes was strong on S. aureus protein pattern showing high degrees of polymorphism. SEM micrographs of S. aureus cells treated with fluoroarylbichalcophenes displayed smaller cell-sizes, fewer numbers, arranged in a linear form and some of them were damaged when compared to the untreated cells. The bioelectrochemical measurements demonstrated the strong sensitivity of S. aureus cells to the tested fluoroarylbichalcophenes and an antibiofilm agent. Eventually, these fluoroarylbichalcophene compounds especially the MA-1156 could be recommended as effective antibacterial agents.

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