Publications by authors named "Baghel D"

Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from Aβ on the structure of the resulting amyloid aggregates is yet to be fully understood.

View Article and Find Full Text PDF

Amyloid aggregates are hallmarks of the pathology of a wide range of diseases, including type 2 diabetes (T2D) and Alzheimer's disease (AD). Much epidemiological and pathological evidence points to significant overlap between AD and T2D. Individuals with T2D have a higher likelihood of developing AD; moreover, colocalized aggregates of amyloid β (Aβ) and the islet amyloid polypeptide (IAPP), the two main peptides implicated in the formation of toxic amyloid aggregates in AD and T2D, have also been identified in the brain.

View Article and Find Full Text PDF

The eye is a most delicate organ protected by several complex biological barriers that are static and dynamic. The presence of these ocular barriers retards drug absorption from topically applied dosage forms at the conjunctival sac. The efficient topical delivery of the drug into the globe is more difficult to achieve and there is a need to develop a topical formulation that may reduce the use of injections and increase patient compliance with decreased frequency of administration.

View Article and Find Full Text PDF

The self-assembly of proteins and peptides into ordered structures called amyloid fibrils is a hallmark of numerous diseases, impacting the brain, heart, and other organs. The structure of amyloid aggregates is central to their function and thus has been extensively studied. However, the structural heterogeneities between aggregates as they evolve throughout the aggregation pathway are still not well understood.

View Article and Find Full Text PDF

Aggregation of the amyloid β (Aβ) peptide into fibrils represents one of the major biochemical pathways underlying the development of Alzheimer's disease (AD). Extensive studies have been carried out to understand the role of fibrillar seeds on the overall kinetics of amyloid aggregation. However, the precise effect of seeds that are structurally or sequentially different from Aβ on the structure of the resulting amyloid aggregates is yet to be fully understood.

View Article and Find Full Text PDF

The aggregation of amyloid β(Aβ) peptides is at the heart of Alzheimer's disease development and progression. As a result, amyloid aggregates have been studied extensively in vitro, and detailed structural information on fibrillar amyloid aggregates is available. However, forwarding these structural models to amyloid plaques in the human brain is still a major challenge.

View Article and Find Full Text PDF

Cerebral amyloid angiopathy (CAA), which involves amyloid deposition in blood vessels leading to fatal cerebral hemorrhage and recurring strokes, is present in the majority Alzheimer's disease (AD) cases. Familial mutations in the amyloid β peptide are correlated to higher risks of CAA and are mostly comprised of mutations at residues 22 and 23. While the structure of the wild-type Aβ peptide has been investigated in great detail, less is known about the structure of mutants involved in CAA and evolutions thereof.

View Article and Find Full Text PDF

Municipal solid waste (MSW) management is getting more attention in the present scenario. Even though various technologies like incineration, gasification, pyrolysis and waste-to-energy plants have been developed, landfills are still the major disposal option for MSW management. MSW at landfill creates issues that are highlighted at a global level like the fire at Deonar dumping site in Mumbai, India was visible and captured by the space satellites, leading to environmental pollution.

View Article and Find Full Text PDF

The aggregation of amyloid beta (Aβ) into fibrillar aggregates is a key feature of Alzheimer's disease (AD) pathology. β-carotene and related compounds have been shown to associate with amyloid aggregates and have direct impact on the formation of amyloid fibrils. However, the precise effect of β-carotene on the structure of amyloid aggregates is not known, which poses a limitation towards developing it as a potential AD therapeutic.

View Article and Find Full Text PDF

Simvastatin (SIM) is known to lower cholesterol levels and is speculated in the pathogenesis of Alzheimer's disease. In this study, the bioanalytical method of SIM SNEDDS was developed and validated for the estimation of SIM in the rat's plasma using reverse-phase high-performance liquid chromatography. C-18 reverse-phase octadecylsilyl column was used to validate the method.

View Article and Find Full Text PDF

Spontaneous aggregation of amyloid beta (Aβ) proteins leading to the formation of oligomers and eventually into fibrils has been identified as a key pathological signature of Alzheimer's disease. The structure of late-stage aggregates have been studied in depth by conventional structural biology techniques, including nuclear magnetic resonance, X-ray crystallography, and infrared spectroscopy; however, the structure of early-stage aggregates is less known due to their transient nature. As a result, the structural evolution of amyloid aggregates from early oligomers to mature fibrils is still not fully understood.

View Article and Find Full Text PDF

Amyloid plaques are one of the central manifestations of Alzheimer's disease pathology. Aggregation of the amyloid beta (Aβ) protein from amorphous oligomeric species to mature fibrils has been extensively studied. However, structural heterogeneities in prefibrillar species, and how that affects the structure of later-stage aggregates are not yet well understood.

View Article and Find Full Text PDF

Purpose: The model biological organism has been utilized to assess the effect of extremely low-frequency electromagnetic field (ELF-EMF) on locomotion, longevity, developmental dynamics, cell viability and oxidative stress.

Materials And Method: Developmental stages of (Oregon R strain) individually exposed to ELF-EMF (75 Hz, 550 T) for 6 h once for acute exposure. For chronic exposure, complete life cycle of fly, that is, egg to adult fly was exposed to ELF-EMF for 6 h daily.

View Article and Find Full Text PDF

Pomegranate ( L.) is an important fruit crop, rich in fiber, vitamins, antioxidants, minerals and source of different biologically active compounds. The bacterial blight caused by pv.

View Article and Find Full Text PDF

Childhood diarrhea continues to be a major cause of under-five (U-5) mortality globally and in India. In this study, 1571 U-5 children residing in nine rural villages and four urban slums in Ujjain, India were included with the objective to use community participation and drug utilization research to improve diarrheal case management. The mean age was 2.

View Article and Find Full Text PDF

Ethnopharmacological Relevance: The genus Anogeissus (axlewood tree, ghatti tree, button tree and chewing stick tree) belongs to Combretaceae, includes eight species that are distributed in Asia and Africa. Plants are used as an ethnomedicine in Asia and Africa to treat various ailments like diabetes, fever, diarrhoea, dysentery, tuberculosis, wound healing, skin diseases (eczema, psoriasis), snake and scorpion venom. Based on the traditional knowledge, different phytochemical and pharmacological activities have been at the focus of research.

View Article and Find Full Text PDF