Taqi Ahmed Khan
Aligarh Muslim University
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Taqi Ahmed Khan.
PLOS ONE | 2013
Afshin Iram; Tauqeer Alam; Javed Masood Khan; Taqi Ahmed Khan; Rizwan Hasan Khan; Aabgeena Naeem
Conformational alterations of bovine hemoglobin (Hb) upon sequential addition of glyoxal over a range of 0–90% v/v were investigated. At 20% v/v glyoxal, molten globule (MG) state of Hb was observed by altered tryptophan fluorescence, high ANS binding, existence of intact heme, native-like secondary structure as depicted by far-UV circular dichroism (CD) and ATR-FTIR spectra as well as loss in tertiary structure as confirmed by near-UV CD spectra. In addition, size exclusion chromatography analysis depicted that MG state at 20% v/v glyoxal corresponded to expanded pre-dissociated dimers. Aggregates of Hb were detected at 70% v/v glyoxal. These aggregates of Hb had altered tryptophan environment, low ANS binding, exposed heme, increased β-sheet secondary structure, loss in tertiary structure, enhanced thioflavin T (ThT) fluorescence and red shifted Congo Red (CR) absorbance. On incubating Hb with 30% v/v glyoxal for 0–20 days, advanced glycation end products (AGEs) were detected on day 20. These AGEs were characterised by enhanced tryptophan fluorescence at 450 nm, exposure of heme, increase in intermolecular β-sheets, enhanced ThT fluorescence and red shift in CR absorbance. Comet assay revealed aggregates and AGEs to be genotoxic in nature. Scanning electron microscopy confirmed the amorphous structure of aggregates and branched fibrils of AGEs. The transformation of α-helix to β-sheet usually alters the normal protein to amyloidogenic resulting in a variety of protein conformational disorders such as diabetes, prion and Huntingtons.
Cns & Neurological Disorders-drug Targets | 2014
Ghulam Md Ashraf; Taqi Ahmed Khan; Iftekhar Hassan; Shams Tabrez; Shazi Shakil; Ishfaq A. Sheikh; Syed Kashif Zaidi; Mohammad Akram; Nasimudeen R. Jabir; Chelaprom K. Firoz; Aabgeena Naeem; Ibrahim M. Alhazza; Ghazi A. Damanhouri; Mohammad A. Kamal
In general, proteins can only execute their various biological functions when they are appropriately folded. Their amino acid sequence encodes the relevant information required for correct three-dimensional folding, with or without the assistance of chaperones. The challenge associated with understanding protein folding is currently one of the most important aspects of the biological sciences. Misfolded protein intermediates form large polymers of unwanted aggregates and are involved in the pathogenesis of many human diseases, including Alzheimers disease (AD) and Type 2 diabetes mellitus (T2DM). AD is one of the most prevalent neurological disorders and has worldwide impact; whereas T2DM is considered a metabolic disease that detrementally influences numerous organs, afflicts some 8% of the adult population, and shares many risk factors with AD. Research data indicates that there is a widespread conformational change in the proteins involved in AD and T2DM that form β-sheet like motifs. Although conformation of these β-sheets is common to many functional proteins, the transition from α-helix to β-sheet is a typical characteristic of amyloid deposits. Any abnormality in this transition results in protein aggregation and generation of insoluble fibrils. The abnormal and toxic proteins can interact with other native proteins and consequently catalyze their transition into the toxic state. Both AD and T2DM are prevalent in the aged population. AD is characterized by the accumulation of amyloid-β (Aβ) in brain, while T2DM is characterized by the deposition of islet amyloid polypeptide (IAPP, also known as amylin) within beta-cells of the pancreas. T2DM increases pathological angiogenesis and immature vascularisation. This also leads to chronic cerebral hypoperfusion, which results in dysfunction and degeneration of neuroglial cells. With an abundance of common mechanisms underpinning both disorders, a significant question that can be posed is whether T2DM leads to AD in aged individuals and the associations between other protein misfolding diseases.
Cns & Neurological Disorders-drug Targets | 2016
Taqi Ahmed Khan; Iftekhar Hassan; Ausaf Ahmad; Asma Perveen; Shazia Aman; Saima Quddusi; Ibrahim M. Alhazza; Ghulam Md Ashraf; Gjumrakch Aliev
Free radicals are generated as byproduct of our body metabolism, and their adverse effect on normal functioning of our body is prevented by bodys own antioxidant machinery. Any perturbation in the defense mechanism of antioxidants inside body, its abnormal production or its induction from environment to our body lead to serious threats and is responsible for the development of various neurodegenerative disorders (NDDs). Perturbed antioxidants result in sensory and functional impairments in neuronal cells, which in turn cause NDDs. Free radical attack on neuronal cells plays a catastrophic role in NDDs. Impaired metabolism and generation of excessive reactive oxygen species also lead to a range of NDDs. Free radical induced toxicity is responsible for DNA injury, protein degradation, damage to tissue inflammation and cell death. Besides various genetic and environmental factors, free radical induced oxidative stress is also a major cause of NDDs. Application of upstream and downstream antioxidant therapy to counter oxidative stress can be an effective option in alteration of any neuronal impairment besides free radical scavenging. In the present manuscript, we have presented a comprehensive update on the symptoms, causes and cures of NDDs in relation with their dynamic association with oxidative stress.
Archive | 2012
Mohd Mazid; Taqi Ahmed Khan; Firoz Mohammad
Amino Acids | 2012
Taqi Ahmed Khan; Samreen Amani; Aabgeena Naeem
International Journal of Agricultural and Food Research | 2014
Mohd Mazid; Taqi Ahmed Khan
The International Journal of Plant, Animal and Environmental Sciences | 2011
Mohd Mazi; Taqi Ahmed Khan; Zeba H. Khan; Saima Quddusi; Firoz Mohammad
Journal of Stress Physiology & Biochemistry | 2011
Mohd Mazid; Taqi Ahmed Khan; Firoz Mohammad
World journal of pharmaceutical research | 2012
Mohd Mazid; Taqi Ahmed Khan; Firoz Mohammad
Journal of Industrial Research & Technology | 2011
Mohd Mazid; Taqi Ahmed Khan; Firoz Mohammad