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In-vitro molecular docking analysis of microalgae extracted phycocyanin as an anti-diabetic candidate
- Source :
- Biochemical Engineering Journal. 161:107666
- Publication Year :
- 2020
- Publisher :
- Elsevier BV, 2020.
-
Abstract
- Phycocyanin (PC) is the main pigment found in Spirulina platensis and has the potential effect to treat effectively type-2 diabetes mellitus by inhibiting α-amylase and α-glucosidase. However, studies on molecular interactions between PC with α-amylase and α-glucosidase enzymes are still rare. In this study, an in-silico study was carried out to predict the molecular interactions between PC with α-amylase and α-glucosidase enzymes. Molecular docking simulations indicated that PC inhibits the enzymes by binding to the active site and causing a disruption on substrate-enzyme binding. In both enzymes, PC seem to play a crucial role in establishing the interaction within the cavity of active sites. This result suggested PC as a potential candidate for antidiabetic natural therapeutic agents. An in-vitro inhibition activity test showed that PC inhibits human salivary amylase at average of 51.13 %. A storage stability tests showed that keeping PC in solid-state, absence of lights and low temperature can preserve the bioactivity when used as functional compounds. Taken together, this current result would be useful in elucidating the molecular mechanisms of the interaction between PC and carbohydrate-metabolisms enzymes and contribute to making full use of PC as antidiabetic drug or therapeutic agent. Further confirm on diabetic subjects is indispensable to provide the potential therapeutic of PC as an effective anti-diabetic with less frequent of side effect.
- Subjects :
- 0106 biological sciences
Drug
chemistry.chemical_classification
0303 health sciences
Environmental Engineering
biology
Side effect
Chemistry
media_common.quotation_subject
Biomedical Engineering
Molecular Docking Analysis
Active site
Bioengineering
01 natural sciences
In vitro
03 medical and health sciences
Enzyme
Biochemistry
010608 biotechnology
Phycocyanin
biology.protein
Amylase
030304 developmental biology
Biotechnology
media_common
Subjects
Details
- ISSN :
- 1369703X
- Volume :
- 161
- Database :
- OpenAIRE
- Journal :
- Biochemical Engineering Journal
- Accession number :
- edsair.doi...........b83d9a00920d314c8381f99f5b38a785
- Full Text :
- https://doi.org/10.1016/j.bej.2020.107666