Research

Ankita Varshney

M. Sc.
Aligarh Muslim University, India

M. Phil
Aligarh Muslim University, India

Ph. D.
Aligarh Muslim University, India

Postdoctoral Research
Jawaharlal Nehru University, New Delhi, India

Email

ankitavarshney@nii.ac.in


Research Interest

Structural Biology & Biophysical Chemistry, Protein-ligand Interaction, Drug-protein Interaction, Protein folding & stability and Popularization of Science         

Summary of Research

Human serum albumin (HSA), being the most abundant carrier protein in blood and a modern day clinical tool for drug delivery, attracts high attention among biologists. HSA acts as a potential contender for being a molecular cargo or nanovehicle for clinical, biophysical and industrial purposes. My work highlights overview on the ligand (drug/non drug) binding and folding/unfolding strategies of the protein in therapeutics and clinical biochemistry. 

Uremic syndrome results from malfunctioning of various organ systems due to the retention of uremic toxins which, under normal conditions, would be excreted into the urine and/or metabolized by the kidneys. We elucidated the complicated mechanism of toxin disposition and impaired drug binding in renal disease state. This is the current interest of the pharmaceutical companies and is extremely important for various diseases such as muscular dystrophy and diabetes.

The heavy environmental pollutants are carcinogenic; albumin is the major transport protein in blood especially for Zn2+ and Cd2+ metal ions as recruited by various drugs and toxins. We probed the binding of anticancerous drug, ganciclovir which have combating effect on HSA and reported the mode of heavy metal toxicity, Zn2+ and Cd2+ proved to affect efficiently the spontaneous binding of ganciclovir inspite of different binding sites to HSA. 

We also elucidated the structural features of multimeric protein, Keyhole Limpet Hemocyanin (KLH) it’s folding and particularly, the dominant role of different intermediate states and the effect of cosolvents in determining the conformations of KLH. Accumulation of these intermediate states is of great significant importance especially in medical sciences since KLH is widely used as an immune stimulant for vaccines immunotherapeutic agent against bladder cancer.

Awards/Fellowships

Biotechnology Career Advancement and Re-orientation Program for Women Scientists, Department of Biotechnology, India (2012)
Dr. D.S. Kothari Postdoctoral Fellowship, University Grants Commission, India (2011)
DBT Research Associateship in Biotechnology and Life Sciences, Department of Biotechnology, India (2011)

Selected Publications

  • Ahmad B; Muteeb G; Alam P; Varshney A; Zaidi N and Khan RH (2015) Thermal Induced Unfolding Of Human Serum Albumin Isomers: Assigning Residual Alpha Helices to Domain II.  Int. J. Biol. Macromol. 75:447-452
  • Varshney A; Rabbani G; Badr G and Khan RH (2014) Cosolvents Induced Unfolding and aggregation of Keyhole Limpet Hemocyanin. Cell Biochem. & Biophy. 69:103-113
  • Varshney A; Ansari Y; Zaidi N; Ahmad E, Badr G; Alam P and Khan RH (2014) Analysis of Binding Interaction between antibacterial ciprofloxacin and human serum albumin by spectroscopic technique. Cell Biochem. & Biophy.70:93-101
  • Varshney A; Rehan M; Subbarao N; Rabbani G and Khan RH (2011) Elimination of Endogenous Toxin Creatinine from Blood Plasma: Site specific Uremic Toxicity and Drug binding. Plos One 6: e17230
  • Varshney A; Sen P; Ahmad E; Rehan M; Subbarao N and Khan RH (2010) Ligand Binding Strategies on Human Serum Albumin: How Can the cargo be Utilized? Chirality 22:77-87
  • Varshney A; Ahmad B; Rabbani G and Khan RH (2010) Acid Induced Unfolding of Didecameric Keyhole Limpet Hemocyanin: Detection and Characterizations of Decameric and Tetrameric Intermediate States. Amino Acids 39:899-910
  • Varshney A; Ahmad B and Khan RH (2008) Comparative studies of Unfolding   & Binding of ligands to Human serum albumin in the presence of fatty acids: Spectroscopic Approach. Int. J. Biol. Macromol. 42:483-490
  • Ahmad B, Ankita and Khan RH (2005) Urea Induced Unfolding of F Isomer of Human Serum Albumin: A Case Study Using Multiple Probes. Arch. Biochem. Biophys. 437:159-167 

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