Search

Interest in edible and medicinal macrofungi is millennial in terms of their uses in health and food products in Central Asia, while interest in inedible and medicinal macrofungi has grown in popularity in recent years. Edible and inedible medicinal basidiomycetes were collected during field surveys from different regions of Uzbekistan. The morphological characters and similarity assessment of rDNA-Internal Transcribed Spacer sequence data were used to measure diversity and habitat associations. A number of 17 species of medicinal macrofungi of ethnomycological and medicinal interest was found associated with 23 species of trees and shrubs belonging to 11 families and 14 genera. Polyporaceae and Hymenochaetaceae were represented by the highest number of species followed by Ganodermataceae, Fomitopsidaceae, Auriculariaceae, Cerrenaceae, Grifolaceae, Phanerochaetaceae, Laetiporaceae, Schizophyllaceae, and Stereaceae. The highest number of medicinal basidiomycete species was reported in the following host genera: Acer, Betula, Celtis, Crataegus, Juglans, Juniperus, Lonicera, Malus, Morus, Platanus, Populus, Prunus, Quercus, and Salix. An updated list of edible and inedible medicinal mushrooms identified in Uzbekistan, their morphological characteristics, and phylogenetic placement are given for the first time. Information is provided on their uses in traditional and modern medicine. Their bioactive compounds and extracts can be applied as medicines, as well as food and cosmetic ingredients. [ABSTRACT FROM AUTHOR]

Human serum albumin (HSA) is the most abundant protein in plasma synthesized by the liver and the main modulator of fluid distribution between body compartments. It has an amazing capacity to bind with multiple ligands, offering a store and transporter for various endogenous and exogenous compounds. Huperzine A (HpzA) is a natural sesquiterpene alkaloid found in Huperzia serrata and used in various neurological conditions, including Alzheimer's disease (AD). This study elucidated the binding of HpzA with HSA using advanced computational approaches such as molecular docking and molecular dynamic (MD) simulation followed by fluorescence-based binding assays. The molecular docking result showed plausible interaction between HpzA and HSA. The MD simulation and principal component analysis (PCA) results supported the stable interactions of the protein–ligand complex. The fluorescence assay further validated the in silico study, revealing significant binding affinity between HpzA and HSA. This study advocated that HpzA acts as a latent HSA binding partner, which may be investigated further in AD therapy in experimental settings. [ABSTRACT FROM AUTHOR]

Parkinsonism-associated deglycase-PARK7/DJ-1 (PARK7) is a multifunctional protein having significant roles in inflammatory and immune disorders and cell protection against oxidative stress. Mutations in PARK7 may result in the onset and progression of a few neurodegenerative disorders such as Parkinson's disease. This study has analyzed the non-synonymous single nucleotide polymorphisms (nsSNPs) resulting in single amino acid substitutions in PARK7 to explore its disease-causing variants and their structural dysfunctions. Initially, we retrieved the mutational dataset of PARK7 from the Ensembl database and performed detailed analyses using sequence-based and structure-based approaches. The pathogenicity of the PARK7 was then performed to distinguish the destabilizing/deleterious variants. Aggregation propensity, noncovalent interactions, packing density, and solvent accessible surface area analyses were carried out on the selected pathogenic mutations. The SODA study suggested that mutations in PARK7 result in aggregation, inducing disordered helix and altering the strand propensity. The effect of mutations alters the number of hydrogen bonds and hydrophobic interactions in PARK7, as calculated from the Arpeggio server. The study indicated that the alteration in the hydrophobic contacts and frustration of the protein could alter the stability of the missense variants of the PARK7, which might result in disease progression. This study provides a detailed understanding of the destabilizing effects of single amino acid substitutions in PARK7. [ABSTRACT FROM AUTHOR]