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.
Original language | British English |
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Article number | 107666 |
Journal | Biochemical Engineering Journal |
Volume | 161 |
DOIs | |
State | Published - 15 Sep 2020 |
Keywords
- Antidiabetic inhibitor
- Bioactivity
- Molecular docking
- Phycocyanin
- Spirulina platensis