School of Biological Sciences
Dr Andy Pickford
- Qualifications: BA (Hons), DPhil
- Role Title: Reader in Molecular Biophysics/ Associate Head (Research)
- Address: King Henry Building, King Henry I Street, Portsmouth, PO1 2DY
- Telephone: 023 9284 2055
- Email: firstname.lastname@example.org
- Department: School of Biological Sciences
- Faculty: Faculty of Science
I graduated from the University of Oxford in 1993 with a BA (Hons) degree in Biochemistry. I went on to complete a DPhil in Biochemistry (1997) in the laboratory of Prof Iain Campbell in Oxford, and continued there as a Research Associate studying the structural biology of the extracellular matrix (ECM) using nuclear magnetic resonance (NMR) spectroscopy as my principal research tool.
I joined the School of Biological Sciences at the University of Portsmouth in September 2005 as Senior Lecturer in Biological NMR. I brought with me extensive experience in the study of the structure, function and dynamic properties of proteins. Since then the focus of my research has turned from the steady-state structure and interactions of the ECM, to the mechanisms by which it is degraded by matrix metalloproteinases (MMPs) – an area of importance in the progression of diseases such as arthritis and cancer. In March 2012, I took on the role of Associate Head (Research) for the School of Biological Sciences.
For more information about my research please visit my lab page
Level 4: Experimental Biology, Perspectives in Biochemistry
Level 5: Macromolecules Biochemistry
Level 6: Biomolecular Science (unit coordinator), Honours Project
Level 7: MRes(Science) project supervisor
Structure-Function Relationships in Matrix Metalloproteinases
Matrix metalloproteinases (MMPs) are a family of zinc-dependant endopeptidases that are important not only in normal physiological processes but also in conditions such as cancer, arthritis and cardiovascular disease. The MMPs are produced as inactive zymogens with an inhibitory pro-domain (PRO) blocking the active site of their catalytic (CAT) domains. The majority of MMPs also possess a hemopexin (HPX) domain which is multifunctional but in most cases allows the enzyme to discriminate between substrates. My research group is interested in answering two specific questions: (1) what is the series of events leading to MMP activation? and (2) what is the molecular mechanism of collagen breakdown (“collagenolysis”) by MMPs? The former question is important because, in many biological systems, MMP synthesis can be upregulated but no proteolysis occurs because the enzyme is inactive. Therefore, MMP activation is the critical step that determines whether tissue breakdown takes place. The latter question is particularly intriguing as the active site cleft in the CAT domain is too narrow to accommodate the collagen triple helix. Thus, the enzyme must somehow unwind the helix prior to hydrolysing the polypeptide backbone. In the Pickford lab, we employ a variety of biophysical methods to perform multi-disciplinary research on the structure-function relationships in MMPs. This is illustrated in our recent article (Arnold et al., 2011) in which, using a combination of analytical ultracentrifugation (AUC), nuclear magnetic resonance (NMR) spectroscopy, surface plasmon resonance (SPR) and small-angle X-ray scattering (SAXS), we found that the interface between the CAT and HPX domains in MMP-1 conceals residues that are important for collagen recognition.