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صفحه اصلی
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4th international edition and 13th Iranian Conference on Bioinformatics
In-silico investigation of bioactive peptides with anti-Alzheimer potential derived from bovine milk αs1-casein protein
نویسندگان :
Mohammad Jahangiri
1
Leila Zarandi-Miandoab
2
1- Department of Biology, Faculty of Sciences, Azarbaijan Shahid Madani University, Tabriz, Iran
2- Department of Biology, Faculty of Sciences, Azarbaijan Shahid Madani University, Tabriz, Iran
کلمات کلیدی :
Bioactive peptides،casein protein،Alzheimer's disease،antioxidant،bioinformatics
چکیده :
Milk is the main source of energy, protein, and fat in the human diet (Gigli, 2016). Cow's milk contains about 32 g of protein per liter, and about 80% of milk protein is casein. αs1-casein is the most abundant casein. Bioactive peptides derived from milk proteins have been the subject of numerous studies in the past two decades due to their various biological properties in human health (Haug, Høstmark and Harstad, 2007). Alzheimer's disease (AD), which has become a global problem due to the aging population and the lack of effective treatments, urgently needs innovative treatments based on natural substances (Wang et al., 2023). According to reliable sources, bioactive peptides with antioxidant properties have anti-Alzheimer's potential (Gupta and Singh, 2024). Also, by inhibiting acetylcholinesterase, it is expected that systemic and circulating acetylcholine levels will increase. Thus, the availability of acetylcholine to stimulate brain receptors for normal cognitive functions will increase. As a result, one of the preferred therapeutic strategies for the management of neurological conditions is the use of acetylcholinesterase (AChE) inhibitors (Ji et al., 2022). The effect of 13 protease enzymes on bovine milk αs1-casein was simulated in silico. In this process, 21 (non-toxic) peptide fragments with antioxidant properties were generated, and the abundance, potential activity, and digestive absorption of these peptides were also investigated. The enzymatic degradation by chymotrypsin A yielded the highest number of antioxidant peptides (5 fragments) compared to other enzymes. Subsequently, a docking test was performed between the obtained antioxidant peptides and the active site of acetylcholinesterase. Comparison of the docking results showed that the highest binding energy was related to the YFYPEL peptide. The results of this study can be used, with further investigation, for the manufacture of drugs or dietary supplements.
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بیشتر
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