Ficus deltoidea leaves extract are known to have good therapeutic properties such as antioxidant, anti-inflammatory and anti-diabetic. We showed that 50% ethanol-water extract of F. deltoidea leaves and its pungent compounds vitexin and isovitexin exhibited significant (p<0.05) αamylase inhibition with IC 50 (vitexin: 4.6 µM [0.02 µg/ml]; isovitexin: 0.06 µg/ml [13.8 µM] and DPPH scavenging with IC 50 (vitexin: 92.5 µM [0.4 µg/ml]; isovitexin: 0.5 µg/ml [115.4 µM]). Additionally, molecular docking analysis confirmed that vitexin has a higher binding affinity (-7.54 kcal/mol) towards α-amylase compared to isovitexin (-5.61 kcal/mol). On the other hand, the molecular dynamics findings showed that vitexin-α-amylase complex is more stable during the simulation of 20 ns when compared to the isovitexin-α-amylase complex. Our results suggest that vitexin is more potent and stable against α-amylase enzyme, thus it could develop as a therapeutic drug for the treatment of diabetes.

Background Neuroinflammation has been identified to be the key player in most neurodegenerative diseases. If neuroinflammation is left to be unresolved, chronic neuroinflammation will be establish. Such situation is due to the overly-activated microglia which have the tendency to secrete an abundance amount of pro-inflammatory cytokines into the neuron microenvironment. The abundance of pro-inflammatory cytokines will later cause toxic and death to neurons. Toll-like receptor 4 (TLR4)/MD-2 complex found on the cell surface of microglia is responsible for the attachment of LPS and activation of nuclear factor-κB (NF-κB) downstream signalling pathway. Albeit vitexin has been shown to possess anti-inflammatory property, however, little is known on its ability to bind at the binding site of TLR4/MD-2 complex of microglia as well as to be an antagonist for LPS. Results The present study reveals that both vitexin and donepezil are able to bind at the close proximity of LPS binding site located at the TLR4/MD-2 complex with the binding energy of − 4.35 and − 9.14 kcal/mol, respectively. During molecular dynamic simulations, both vitexin and donepezil formed stable complex with TLR4/MD-2 throughout the 100 ns time length with the root mean square deviation (RMSD) values of 2.5 Å and 4.0 Å, respectively. The root mean square fluctuation (RMSF) reveals that both compounds are stable. Interestingly, the radius of gyration (rGyr) for donepezil shows notable fluctuations when compare with vitexin. The MM-GBSA results showed that vitexin has higher binding energy in comparison with donepezil. Conclusions Taken together, the findings suggest that vitexin is able to bind at the binding site of TLR4/MD-2 complex with more stability than donepezil throughout the course of 100 ns simulation. Hence, vitexin has the potential to be an antagonist candidate for LPS.

Major ampullate spidroin (MaSps) from orb-weaver spp spider has recently gained interest due to its exceptional characteristics. The biomechanical and biochemical properties from MaSps offer potential in harvesting and exploiting MaSps as a promising bio-based product. However, the current research on the structural elucidation focused more onto the Nephila clavipes spider web rather than the Nephila pilipes which are more common in this region. Herein, this study integrates the used of computational power and algorithm to elucidate the 3D protein morphology of MaSp1 and MaSp2 of Nephila pilipes dragline silk protein using nearly complete amino acid sequences obtained from the protein database. In silico homology modelling via Phyre2, SWISS-MODEL and RaptorX was adopted to predict the protein structure of MaSP-1 and 2 using proteins threading, automated comparative modelling of three-dimensional (3D) protein structures and deep learning approaches. Consequently, we described a thorough 3D protein models of MaSp1 and MaSp2 with a higher percentage of coils, α-helix and a low percentage of β-sheet on repetitive regions of MaSp1 and MaSp2. The results of this current work provide insights into Bioinformatics potentials in engineering spider silk-based biomaterial and bridging the most apparent gaps in the knowledge of MaSp1 and MaSp2.

Ficus deltoidea (Moraceae), Mas cotek, is a local medicinal plant which has been used for its health benefits including antioxidant, improving blood circulation and anti-hypertension effects. This study aims to determine the vitexin and isovitexin content in various varieties of F. deltoidea, and to study the extract's inhibitory effect on angiotensin converting enzyme (ACE) activity as anti-hypertension marker. Five varieties were studied including F. deltoidea var deltoidea, F. deltoidea var. angustifolia, F. deltoidea var tranguensis, F. deltoidea var. Telinga Beruk, and F. deltoidea var. Tapak Itik. Five extracts were prepared; water, methanolic, ethanolic, 50% methanolic and 50% ethanolic, and ACE inhibitory effect was studied in vitro. Vitexin and isovitexin concentration was in the range 0.001-0.35% and 0.001-7.025% (w/w), respectively. The highest ACE inhibition was obtained from F. deltoidea var. Tapak Itik (FD-TI) extracts where the 50% ethanolic and 50% methanolic extracts showed the most promising results. A bivariate correlation analysis may indicate existence of relation between vitexin in FD extracts and the ACE inhibition (r = 0.58), whereas the isovitexin results do not show any relationship (r= -0.06). The median inhibitory concentration (IC 50 ) of the 50% ethanolic extract of FD-TI was 22±3.8µg/ml, and that of vitexin and isovitexin was 3.1±0.5µg/ml, 18.6±1.3µg/ml, respectively. Our results showed the ACE inhibitory effect is partly due to existence of vitexin but not isovitexin, and the 50% ethanolic extract of the F. deltoidea var. Tapak Itik as a possible antihypertension candidate.

Dysregulation of matrix metalloproteinases (MMPs) activity is known in many pathological conditions with which most of the conditions are related to elevate MMPs activities. Ficus deltoidea (FD) is a plant known for its therapeutic properties. In order to evaluate the therapeutic potential of FD leaf extract, we study the enzymatic inhibition properties of FD leaf extract and its major bioactive compounds (vitexin and isovitexin) on a panel of MMPs (MMP-2, MMP-8 and MMP-9) using experimental and computational approaches. FD leaf extract and its major bioactive compounds showed pronounced inhibition activity towards the MMPs tested. Computational docking analysis revealed that vitexin and isovitexin bind to the active site of the three tested MMPs. We also evaluated the cytotoxicity and cell migration inhibition activity of FD leaf extract in the endothelial EA.hy 926 cell line. Conclusively, this study provided additional information on the potential of FD leaf extract for therapeutical application.