With my highly advanced skills, and vision I have had developed over the years, I believe my inclusion would be of great significance for any global top 10 University/Research Institute). Such an institute would become an ideal platform for me to learn and transmit novelty across in the chosen field. By working with leading researchers and professors, I would be able to envision what new I can assimilate in the field and how can I improve already gained skill and knowledge in the specified field of my expertise coupled with professional growth. This is the perspective that would make me globally prospective and would be in the fitness of things for industry/academia to have a potential candidate around who would be in a position to help industry/research lab/academic teach, create, innovate and commercialize molecular/cell-based/bioelectronic therapeutic solutions for improving the standard of healthcare globally.

I would like to embark on a research and development career with commercial promise and significantly endeavored to human welfare. Therefore ideally, in an academic setup, I would like to work at the interface of both academia and industry. The GlaxoSmithKline (gsk), AstraZeneca, Pfizer, Novartis and Bristol Meyers Squibb etc are key research industries I would like to work with and develop along.

British Council, UK (£1500)

Hammond Trust (£500)

The Leche Trust (£2000)

Honourable Chief Minister (appreciation award £2000)

Honourable Governor (£2000)

Honourable Chief Minister (£2000)

One of the top three candidates shortlisted and called for an interview from amongst a total of 18 candidates who applied Worldwide for the Postdoctoral Position in the University of Cambridge, UK (2014). The project was aimed at the development of aggregation based assays for the detection of cancer.

Selected for an interview for three-year Postdoctoral Position in the University of Nottingham, UK (2013). The project was aimed at the development of antibody-based drugs.

Selected for an interview for the position of Research Associate at KTP Randox Laboratories, Queen's University of Belfast, UK (2013)

a. Attended several hi-tech scientific workshops such as how smart molecules can be turned into business?
b. Held meetings with senior fellows from multidisciplinary fields for potential collaborations/positions
c. Frequently visited Central Library and other libraries around for browsing periodicals/journals online and relevant books
d. Developed some professional contacts
e. Visited few labs and attended couple of interviews as well​

Research project: Extraction, characterization, binding activity and structural analysis of survivin protein (associated with many cancers).

I provide protein size characterization and structural analysis expertise within a larger project team, the work involved E.coli cell culture, cell transformation, protein expression and protein
purification.

Appropriate formulation conditions are currently identified utilizing range of analytical techniques employed for the detection and quantification of aggregates. The current standard for this is size- exclusion chromatography although, due to range of reported problems, recent years have seen the application of a range of other approaches, including sedimentation velocity and light scattering. Using these techniques, typically the optimal formulation is identified through evaluation of aggregate level in a wide range of test formulations that have been exposed to different storage conditions. Here it was attempted to develop a step change to this strategy and develop novel platforms based on the detection of aggregation at nanoscale, to allow rapid screening and identification of optimal formulation conditions. Initial studies focused on the development of an assay to screen for optimal formulation conditions to prevent aggregation in solution. A potential format exploited was build on that developed by the group of Engel for high resolution imaging of membrane proteins (Muller 1999), Biophysics.J. 76,1101. To develop this approach for protein aggregation screening, AFM probes were used to image proteins and an improved control of probe surface interaction area was achieved by optimizing the different imaging parameters. Forces were recorded by bringing the AFM probe into and out of contact, at frequent spatial location intervals, with a sample surface functionalized with biomolecule of interest. The protein (antibody) formulations with sugars at different ratios were analyzed for particle size by Nanosight, DLS, and atomic force microscopy AFM. AFM/SEM were also employed to identify and characterize different components in the lyophilized formulations. DSC and ATR - FTIR spectroscopy were also used to identify any structural changes.

Several factors such as load, temperature and attachment chemistry have the potential to influence unbinding forces in single molecule measurements. Most single molecule force spectroscopic studies within the literature have investigated bonding strength on the basis of loading rate (which can be varied through measurement rate and the mechanical properties of the immobilization chemistry). Few studies have taken into account the critical effect of an increase in temperature. In this work, the temperature dependence of single molecule force spectroscopy measurements has been explored. It was observed that the unbinding forces of both streptavidin-biotin and complementary DNA oligonucleotides decrease with temperature. The decrease in the unbinding force of both molecular species was attributed to the increase in the thermal energy of the system, which tilts the energy binding energy landscape in the direction of applied force besides decreasing the thermal force scale. Moreover increase in thermal energy decreases thermal off rate exponentially. The combined effect of all these factors reduces the unbinding forces of both the studied systems. However, for DNA, temperature increases are also known to decrease the average fraction of bonded pairs in hybridised DNA duplexes, which in these experiments would result in an additional reduction in force.

The presented data hence provide new insight into the effect of temperature on single molecule force spectroscopy data and the opportunities presented by a novel dendron based immobilization strategy.

Numerous biomolecular immobilization methods (such as salinization) are available to attach interacting molecules with the probe and surface. The only purpose of biomolecular immobilization is to produce all the suitable conditions such as sufficient mesospacing, no formation of aggregates, minimal steric hindrance between the interacting molecules, enhanced specific and single molecule interaction, and least possible non-specific interaction etc) necessary for the complete detection of all the mechanical events like DNA hybridisation, protein folding-unfolding, etc on a nanoscale level. Any immobilization approach should provide us with all the relevant surface characteristics for DFS and should be reproducible. Dendron immobilization approach in this regard has been found to be one of the promising candidates, as because it not only provides all the relevant surface characteristics needed for the proper investigation of biomolecules but also has tremendous potential to serve in other biological applications. The dendritic polymers can differ significantly from linear polymers in their properties. They have a number of beneficial attributes for biomedical applications, including the biodistribution and pharmacokinetic properties that can be tuned by controlling dendrimer size and conformation. This can be achieved with precision by varying dendrimer generation number or by creating dendrimer-polymer hybrids, high structural and chemical homogeneity. Dendrimer biological properties can be attributable to a single molecular entity and not a statistical distribution of polymeric or self-assembled materials, facilitating the reproducibility of pharmacokinetic data within and between different synthetic lots. Unlike in linear polymers, as a dendrimer's generation increases, the multivalent ligand density at the surface increases, which can strengthen ligand-receptor binding and improve the targeting of attached components.

The peculiar feature of nanotechnology is its multi-disciplinarity and its coverage is vast and illusive, because of its potential to do wonders in almost all the vibrant and diverse scientific disciplines. Remarkable breakthroughs have been witnessed in bio-engineering, molecular biology, diagnostics, therapeutics etc. [1] [2], [3] Advancement in this highly prospective field of science can discover innovative methodologies for the development and production of functional and effective nano-systems by way of surface modification, incorporation, adsorption or covalent coupling of bio-polymers like carbohydrates, proteins, nucleic acids, endogenous substances etc to the surface of nanoparticles. Functionalisation bestows a wide range of exciting properties such as bio-adhesive property, prevents formation of aggregates by nanoparticles, bioavailability, biostability and solubility, reduces toxicity, improves efficacy of drug and site-specific delivery. [4] This is what makes a nanosystem an important and advanced tool for accurate diagnostics, prognostics and controlled and sustained delivery of proteins, peptides, DNA, RNA or any other substance in the form of nanoparticles. Nanoparticles as drug carriers can effectively improve the therapeutic efficacy of the encapsulated drug by enhancing and sustaining the drug delivery in the target cell. [4] Sound number of nanoparticles has been found to deliver drugs inside the target cells effectively for controlling and eradicating the complicated implications of the biological and bio-medical problems. By putting nanomaterials into bio-medical application gives birth to a new dimension of nanotechnology called nanomedicine. Nanomaterials can be either organic (having living source) or inorganic (non-living source). The best source of inorganic nanomaterial is carbon nanotube (CNT), which is considered to be super novel material, set to revolutionise all the sectors of life, ranging from materials to medical science.

Nottingham University is Top 10 UK University and has given World an MRI and Ibuprofen, courtesy Prof. Sir Peter Mansfield and Dr Stewart Admas respectively. I have been privileged to meet both scientists during my stay at the Nottingham University. In particular, Nanotechnology Center (NNNC) and Laboratory of Biophysics and Surface Analysis (LBSA) have made significant contributions in honing my scientific skills and research acumen to gain an expertise which has shaped my scientific career on the global stage.

After joining the University of Nottingham’s Nanoscience and Nanotechnology Center (NNNC) in the year 2007, I received novel scientific education and advanced training in the field of Nanoscience and Nanotechnology as well as the accomplishment of a full-time Masters of Research (MRes) in Single Molecule Nanotechnology which was bestowed to me with Distinction.

In the year 2009, Mudasir subsequently moved to Laboratory of Biophysics and Surface Analysis (LBSA), a Research Division of the School of Pharmacy [(Top Ranked in the UK (RAE 2008); 10th global best in 2014)]; from where I gained PhD in Pharmaceutical Nanotechnology/Biotherapeutic Formulation under the valuable supervision of Pro Vice-Chancellor Prof. Saul Tendler, Director Nanotechnology Centre Prof. Clive Roberts and Prof. Stephanie Allen.

Olberon Ltd a medical device innovations company based in Nottingham UK, specialising in Venous Access and Diagnostic devices. Olberon's medical devices originate from direct experience of patient care with an emphasis on improving problematic medical procedures for both patient and practitioner. With this approach, Olberon are able to design truly useful medical innovations that improve efficiency for the practitioner, provide a better experience for the patient with simple easy to use designs that aid existing medical procedures and reduce costs to the NHS and other healthcare authorities with improved medical device innovations.

I worked with them for the product Vacuderm Tourniquet. I did the following:

Prepared clinical summary reports and performed statistical data analysis.
Contributed to medical device description, labelling and market evaluation
Labelled and described newly designed medical devices such as Vacuderm Tourniquet to GPs

The product Vacuderm Tourniquet used for Phlebotomy is now on the market
Held meetings with regulatory authorities for product approval.

Queen's Medical Center (QMC) is an associated hospital of Nottingham University, based in the heart of Nottingham and provide services to over 2.5 million residents of Nottingham and its surrounding communities. QMC also provides specialist services for a further 3-4 million people from across the region.

I was involved in the research project revolving around survivin protein. The project involved extraction, characterization, binding activity and structural analysis of survivin protein (associated with many cancers). Provided protein size characterization and structural analysis expertise within a larger project team, the work involved E.coli cell culture, cell transformation, protein expression and protein purification.