Marco Albanese

Name: Marco Albanese

Oxford Drug Design
Oxford Centre for Innovation
New Road, Oxford

Education and Experience

In February 2018, I completed my Master’s degree in Pharmaceutical Chemistry and Technology at the University of Salerno. Throughout this five-year degree, I gained a deep understanding of the challenging field of drug discovery. I acquired fundamental multidisciplinary knowledge of chemistry, biology, pharmacology necessary to the understanding of a drug, its structure and its interaction with biological systems, and all the activities required to prepare and carry out controls on pharmaceutical products.

My interest in computer-aided drug design grew up at the University of Eastern Finland, where I studied for nine months as an exchange student. Under the supervision of prof. Antti Poso, I led my first molecular modelling project with the aim to identify inhibitors of SUMO E2 conjugating enzyme UBC9 by using a WaterMap-based ensemble docking.

Back to Italy, I joined the organic chemistry group of prof. Giuseppe Bifulco where I completed my Master’s thesis entitled “Application of Computational Methods to the Design of Potential Anti-inflammatory and Anti-cancer Compounds”. As part of this project, I performed a fragment-based in silico screening to inhibit the microsomal prostaglandin E synthase-1 (mPGES-1), and I successfully optimized an allosteric binder of Macro Domain 1. Working on several targets gave me the chance to apply different approaches, to learn their strengths and limitations 

ESR1 – Computational Models of Histidine Kinases and their Inhibitors.

My project
Novel first in class antibiotics are urgently needed to address the rise of multidrug-resistant bacteria. Bacterial Histidine Kinases (HKs) are a potential therapeutic target given their involvement in a wide range of sensing pathways including those related to resistance, virulence and metabolism. HK’s catalytic core comprises the catalytic and ATP-binding (CA) domain and the dimerization and histidine phosphotransfer domain.

With the aim to identify compounds with broad-spectrum activity, our computer-aided drug discovery strategy focused on the design of inhibitors targeting the conserved catalytic and ATP-binding domain. This approach should result in the simultaneous inhibition of several sensing pathways (polypharmacology). For instance, Staphylococcus aureus encodes 16 HKs and more than 60 HKs are found in Pseudomonas aeruginosa, both clinically relevant pathogens. While affecting bacterial fitness, a polypharmacological approach is predicted to reduce the emergence of target-based resistance.

By using proprietary and commercial molecular modelling tools, we aim to: I) identify the critical features required for binding to histidine kinase; II) identify novel inhibitors; III) optimize their pharmacokinetic/pharmacodynamic properties in collaboration with chemistry (ESR3) and biology (ESR2 and ESR4) colleagues.