Molecular Basis of the Anti-Diabetic Properties of Camel Milk Through Profiling of Its Bioactive Peptides on DPP-IV and Insulin Receptor Activity

Author(s):  
Arshida Ashraf ◽  
Priti Mudgil ◽  
Abdulrasheed Palakkott ◽  
Rabah Iratni ◽  
Chee-Yuen Gan ◽  
...  

2021 ◽  
Vol 104 (1) ◽  
pp. 61-77
Author(s):  
Arshida Ashraf ◽  
Priti Mudgil ◽  
Abdulrasheed Palakkott ◽  
Rabah Iratni ◽  
Chee-Yuen Gan ◽  
...  


2021 ◽  
Vol 22 (17) ◽  
pp. 9508
Author(s):  
Nhung Thi Phuong Nong ◽  
Jue-Liang Hsu

Diabetes, a glucose metabolic disorder, is considered one of the biggest challenges associated with a complex complication of health crises in the modern lifestyle. Inhibition or reduction of the dipeptidyl peptidase IV (DPP-IV), alpha-glucosidase, and protein-tyrosine phosphatase 1B (PTP-1B) enzyme activities or expressions are notably considered as the promising therapeutic strategies for the management of type 2 diabetes (T2D). Various food protein-derived antidiabetic bioactive peptides have been isolated and verified. This review provides an overview of the DPP-IV, PTP-1B, and α-glucosidase inhibitors, and updates on the methods for the discovery of DPP-IV inhibitory peptides released from food-protein hydrolysate. The finding of novel bioactive peptides involves studies about the strategy of separation fractionation, the identification of peptide sequences, and the evaluation of peptide characteristics in vitro, in silico, in situ, and in vivo. The potential of bioactive peptides suggests useful applications in the prevention and management of diabetes. Furthermore, evidence of clinical studies is necessary for the validation of these peptides’ efficiencies before commercial applications.





2018 ◽  
Vol 4 (3) ◽  
pp. 273-280 ◽  
Author(s):  
Hisham R. Ibrahim ◽  
Hiroki Isono ◽  
Takeshi Miyata


2000 ◽  
Vol 6 (6) ◽  
pp. 1401-1412 ◽  
Author(s):  
Annette Salmeen ◽  
Jannik N Andersen ◽  
Michael P Myers ◽  
Nicholas K Tonks ◽  
David Barford


2017 ◽  
Vol 24 (2) ◽  
pp. 181
Author(s):  
Maryam Salami ◽  
Amir Niasari-Naslaji ◽  
A. Ali Moosavi-Movahedi


2021 ◽  
pp. 131444
Author(s):  
Ali Ali Redha ◽  
Hamidreza Valizadenia ◽  
Shahida Anusha Siddiqui ◽  
Sajid Maqsood


Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2910 ◽  
Author(s):  
Fenny Panjaitan ◽  
Honey Gomez ◽  
Yu-Wei Chang

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.



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