Time filter

Source Type

Owais M.,Interdisciplinary Biotechnology Unit
Current gene therapy | Year: 2015

RNAi based therapeutics hold s great promises to be an efficient strategy of the anti-gene realm in context of its therapeutic applications; however, despite significant potentials, its full efficacy cannot be realized in real sense owing to various confronts that plague its advancement. Efforts need to be driven for the development of specific and efficacious strategies to subdue some of their crucial constraints towards successes in clinics. This article will present the major impediments that encumber successful translation of siRNA concept into reality and the ongoing research endeavours to get through those stumbling blocks along with their inadequacies. Source

Rehman M.T.,Interdisciplinary Biotechnology Unit | Rehman M.T.,King Saud University
Journal of Biomolecular Structure and Dynamics | Year: 2016

Cystatins, known for their ubiquitous presence in mammalian system are thiol protease inhibitors serving important physiological functions. Here, we present a variant of cystatin isolated from brain of Capra hircus (goat) which is glycosylated but lacks disulphide bonds. Caprine brain cystatin (CBC) was isolated using alkaline treatment, ammonium sulphate fractionation (40–60%) and gel filtration chromatography on Sephacryl S-100HR column with an overall yield of 26.29% and 322-fold purification. The inhibitor gave a molecular mass of ~44 kDa as determined by SDS-PAGE and gel filtration behaviour. The Stokes radius and diffusion coefficient of CBC were 27.14 Å and 8.18 × 10−7 cm2 s−1, respectively. Kinetic data revealed that CBC inhibited thiol proteases reversibly and competitively, with the highest inhibition towards papain (Ki = 4.10 nM) followed by ficin and bromelain. CBC possessed 34.7% α-helical content as observed by CD spectroscopy. UV, fluorescence, CD and FTIR spectroscopy revealed significant conformational change upon CBC-papain complex formation. Isothermal titration calorimetry (ITC) was used to measure the thermodynamic parameters – ΔH, ΔS, ΔG along with N (binding stoichiometry) for CBC-papain complex formation. Binding stoichiometry (N = .97 ± .07 sites) for the CBC-papain complex indicates that cystatin is surrounded by nearly one papain molecule. Negative ΔH (−5.78 kcal mol−1) and positive ΔS (11.01 cal mol−1 deg−1) values suggest that the interaction between CBC and papain is enthalpically as well as entropically favoured process. The overall negative ΔG (−9.19 kcal mol−1) value implies a spontaneous CBC-papain interaction. © 2016 Informa UK Limited, trading as Taylor & Francis Group Source

Khan A.U.,Interdisciplinary Biotechnology Unit
Asian Pacific Journal of Tropical Medicine | Year: 2010

Recently WHO has again declared Influenza pandemic due to the outbreak of H1N1 which has infected over 254,206 people in 80 countries, with 625 deaths. Our lab has started working on the proteome analysis of H1N1, 2009 out break strains. © 2010 Hainan Medical College. Source

Khan A.U.,Interdisciplinary Biotechnology Unit | Khan A.U.,University Paris - Sud | Nordmann P.,University Paris - Sud
Scandinavian Journal of Infectious Diseases | Year: 2012

New Delhi metallo-β-lactamase 1 (NDM-1) producers, first identified from patients hospitalized in India, are now reported worldwide. The Indian subcontinent is clearly a main reservoir of NDM-1 producers. In order to slow down the spread of these NDM-1-positive Enterobacteriaceae, first in India and then worldwide, a series of measures must be implemented as soon as possible. These include discouraging the over-the-counter sale of antibiotics, improving basic and extended knowledge on hygiene, and the wide-scale detection of blaNDM-1, in both infecting agents and in the carrier state for at-risk patients. © 2012 Informa Healthcare. Source

Salahuddin P.,Interdisciplinary Biotechnology Unit | Fatima M.T.,Indian Institute of Science | Abdelhameed A.S.,King Saud University | Nusrat S.,Interdisciplinary Biotechnology Unit | Khan R.H.,Interdisciplinary Biotechnology Unit
European Journal of Medicinal Chemistry | Year: 2016

Protein misfolding is one of the leading causes of amyloidoses. Protein misfolding occurs from changes in environmental conditions and host of other factors, including errors in post-translational modifications, increase in the rate of degradation, error in trafficking, loss of binding partners and oxidative damage. Misfolding gives rise to the formation of partially unfolded or misfolded intermediates, which have exposed hydrophobic residues and interact with complementary intermediates to form oligomers and consequently protofibrils and fibrils. The amyloid fibrils accumulate as amyloid deposits in the brain and central nervous system in Alzheimer's disease (AD), Prion disease and Parkinson's disease (PD). Initial studies have shown that amyloid fibrils were the main culprit behind toxicity that cause neurodegenerative diseases. However, attention shifted to the cytotoxicity of amyloid fibril precursors, notably amyloid oligomers, which are the major cause of toxicity. The mechanism of toxicity triggered by amyloid oligomers remains elusive. In this review, we have focused on the current knowledge of the structures of different aggregated states, including amyloid fibril, protofibrils, annular aggregates and oligomers. Based on the studies on the mechanism of toxicities, we hypothesize two major possible mechanisms of toxicities instigated by oligomers of Aβ (amyloid beta), PrP (prion protein) (106-126), and α-Syn (alpha-synuclein) including direct formation of ion channels and neuron membrane disruption by the increase in membrane conductance or leakage in the presence of small globulomers to large prefibrillar assemblies. Finally, we have discussed various novel innovative approaches that target amyloid oligomers in Alzheimer's diseases, Prion disease and Parkinson's disease. © 2016 Elsevier Masson SAS. All rights reserved. Source

Discover hidden collaborations