Rohanah Hussain
Circular Dichroism
Rohanah Hussain is a beamline scientist on Circular Dichroism Beamline B23. Rohanah’s main interest resides in the field of biopharmaceuticals in drug design and delivery and novel applications of analytical techniques in the field of life sciences. Her work has covered drug interaction, macromolecular interaction, structural-activity, quality control, protein folding, secondary structure, conformational changes and enzyme mechanisms.
Research in this field involves the study of biomolecular interactions where the scientific applications of B23 will play a major role.
Email: Rohanah Hussain
Tel: +44 (0) 1235 778524
Beamline B23: Circular Dichroism
Key Research Areas
Pharmaceutical chemistry and formulation, drug design, optical spectroscopy
Current Research Interests
One of the benefits of understanding molecular recognition is the ability to use structural information to determine affinities of binding interactions. In drug design, formulation or delivery, structural information of potential drug targets and biological environments such as solvents, receptors and membranes are of paramount importance. Delivery of a drug to the target site to initiate therapeutic effect poses a major challenge. Our research focuses on an albumin based delivery system that aims to address this need.
Serum albumin is known to bind a large variety of drugs and has been associated with poor pharmacokinetic performance and diminished efficacy. We have developed an albumin-based delivery system that exploits these binding characteristics to control the serum stability and drug solubility of a broad range of compounds. We have identified a strategy on how the strength of association of a lipophilic drug to albumin may be tuned. Once administered, the formulated complex provides a reservoir of drug for release into the circulation. Our delivery system has application to therapeutic drugs that contain lipid components or that can be lipid-labelled whilst retaining activity. These drugs have presented formulation challenges, as their lipid characteristics give rise to solubility problems.
In addition, the formulation system also confers additional stability on peptide, lipo-peptide and peptide-derived drugs. Consequently, the technology offers a potential mechanism of capitalising on the promise of peptide based therapeutics and provides a formulation solution to the stability problems that have limited their clinical development.
The approach is suitable for parenteral administration, and may be extended to address the need for inhalation formulation solutions. The technology is tuneable, enabling the circulating times to be modulated and designed into the drug formulation system. The albumin formulation system does not add significant risk to the therapeutic development cycle and exploits material that is well established in the clinical setting.
Concurrently, arising from work on peptide antimicrobial interactions with bacterial membranes, we initiated an antimicrobial peptide design programme to tackle the MRSA problem. The drug design aims to circumvent the potential bacterial resistance problem that will arise with antibiotics via interaction on the bacterial membrane. This antimicrobial drug design exploits the existing in-house formulation system for better drug delivery with increased efficacy.
Selected Publications
- Identification and Characterization of Novel Lipophilic Antimicrobial Peptides Derived from Naturally Occurring Proteins, Rohanah Hussain, Christopher L. Joannou and Giuliano Siligardi, International Journal of Peptide Research and Therapeutics, 2006,12 (3), 269 - 273
- Fat-free Albumin as a Novel Drug Delivery System, Rohanah Hussain and Giuliano Siligardi, International Journal of Peptide Research and Therapeutics, 2006,12 (3), 311 - 315
- 4-Fluoroproline derivative peptides: effect on PPII conformation and SH3 affinity, P Ruzza, G Siligardi, A Donella-Deana, A Calderan, R Hussain, C Rubini, L Cesaro, A Osler, A Guiotto, L A. Pinna and G Borin, J. Peptide Science, 2006, 12 (7), 462-471
- Structure and Association of Human Lactoferrin Peptides with the Lipopolysaccharide of Escherichia coli, D.S. Chapple, R Hussain, C.L. Joannou, R.E.W. Hancock, E Odell, R.W. Evans, G. Siligardi, Antimicrobial Agents and Chemotherapy 2004, 2190-2198.