The effects of herbal plant extract on the growth performance, blood parameters, nutrient digestibility and carcase quality of rabbits: A meta-analysis.

A meta-analysis was conducted to determine the effects of herbal plant extracts on the growth performance, blood parameters, nutrient digestibility and carcase quality of farmed rabbits. A dataset was created from 33 in vivo studies comprising 121 experimental units. Statistical meta-analysis was performed using a random-effects model and linear-mixed model meta-regression using R software (v. 4.3.0). Our results showed that although supplemental herbs did not affect average daily gain (ADG) and final body weight (BW), they reduced (P < 0.01) feed conversion ratio and mortality and increased the digestibility of dry matter (DM) (P = 0.014) and crude protein (CP) (P = 0.018). The herbal extracts also increased (P = 0.037) blood high-density lipoprotein (HDL) and decreased (P = 0.004) low-density lipoprotein (LDL). Immunoglobulin M (IgM) was elevated (P = 0.009) by herbal plant extract supplementation, although most blood components were unaffected. The inclusion of herbal plant extract up to 300 g/kg increased (P = 0.011) carcase percentage while the weight and percentage of other organs were unaffected. Subgroup meta-analysis further explained the different effect of the type of herbal plant extract. Moringa, olive oil, and pepper were more favourable to increase final BW compared to the other herbs. Interestingly, the majority of herbs showed efficacy in reducing mortality. A majority of the response variables in our meta-analysis showed no dose-response effect except for ADG, mortality, HDL, and LDL which were improved by herbs supplementation. The evidence from the perspective of both meta-analysis and meta-regression shows that the addition of herbs tends to positively affect the parameters for production performance and blood metabolites in farmed rabbits.

Dysfunctional energy and future perspective of low dose H2O2 as protective agent in neurodegenerative disease.

The number of people with neurodegenerative disease continues to increase every year. A new perspective is needed to overcome this disease. In this review, researchers collected information about dysfunctional energy in neurodegenerative diseases driven by mitochondria. Mitochondrial dysregulation can cause damage to the neuron system. The increase in the amount and interaction of α-synuclein with SAMM50 and GABARAPL1 in the mitochondria is one of the factors causing neurodegenerative disease. As an energy provider in the body, the existence of harmonization in the regulation of mitochondria, specifically the mitochondrial outer membrane, is important. Low-dose hydrogen peroxide (H2O2) has neuroprotective abilities to overcome the impairment function of mitochondria in neurodegenerative patients. Based on computational simulation of this case, it can be used as a basic concept for the development of the role of H2O2 in neurodegenerative diseases.

Quantification and Improvement of the Dynamics of Human Serum Albumin and Glycated Human Serum Albumin with Astaxanthin/Astaxanthin-Metal Ion Complexes: Physico-Chemical and Computational Approaches.

Glycated human serum albumin (gHSA) undergoes conformational changes and unfolding events caused by free radicals. The glycation process results in a reduced ability of albumin to act as an endogenous scavenger and transporter protein in diabetes mellitus type 2 (T2DM) patients. Astaxanthin (ASX) in native form and complexed with metal ions (Cu2+ and Zn2+) has been shown to prevent gHSA from experiencing unfolding events. Furthermore, it improves protein stability of gHSA and human serum albumin (HSA) as it is shown through molecular dynamics studies. In this study, the ASX/ASX-metal ion complexes were reacted with both HSA/gHSA and analyzed with electronic paramagnetic resonance (EPR) spectroscopy, rheology and zeta sizer (particle size and zeta potential) analysis, circular dichroism (CD) spectroscopy and UV-Vis spectrophotometer measurements, as well as molecular electrostatic potential (MEP) and molecular docking calculations. The addition of metal ions to ASX improves its ability to act as an antioxidant and both ASX or ASX-metal ion complexes maintain HSA and gHSA stability while performing their functions.

DFT and molecular dynamics studies of astaxanthin-metal ions (Cu2+ and Zn2+) complex to prevent glycated human serum albumin from possible unfolding.

Glycated human serum albumin (gHSA) undergoes conformational changes of proteins caused by free radicals. The glycation process results in a reduced ability of albumin as an endogenous scavenger in diabetes mellitus type 2 (T2DM) patients. Astaxanthin (ASX) has been shown to prevent gHSA from experiencing unfolding events and improve protein stability of gHSA and HSA through molecular dynamics. In this study, astaxanthin is complexed with transition metal ions such as copper (Cu2+) and zinc (Zn2+) in two modes (M) and (2M). Complexing astaxanthin with Cu2+ and Zn2+ is expected to increase astaxanthin's ability as an endogenous scavenger than in native form. This research aims to characterize the antiradical property of ASX, ASX-Cu2+ and ASX-2Cu2+, ASX-Zn2+, and ASX-2Zn2+ with density functional theory (DFT) and to compare the capability to prevent conformational changes on glycated albumin through molecular dynamics simulation. DFT as implemented in Gaussian 09W, was used for all calculations. Analysis of data using GaussView 6.0. LANL2D2Z basis set and B3LYP density functional used for frequency analysis and optimization. The AutoDock Vina implemented in PyRx 0.8 is used to and receptor-ligand interactions analysis with the DS 2016 Client. YASARA for molecular dynamic simulation with 15,000 ps as running time. DFT analyzes such as energy gaps, HOMO, and LUMO patterns and electronic properties have shown that ASX-metal ions complex is better than ASX in native state as antioxidants. These results are also supported by the molecular dynamics simulation (RMSD backbone, RMSDr, RMSFr, and movie visualization), where the addition of ASX-metal ions complex on gHSA are better than ASX as a single compound in preventing gHSA from possible unfolding and maintaining protein molecule stability.