Located between
Cambridge and Lisbon,
our laboratory works
at the interface of Chemistry
and Biology, with a focus
on protein chemistry and
targeted cancer therapeutics.

LATEST NEWS

July 2018

Chemistry World highlights our last study on β-lapachone, an allosteric inhibitor for 5-lipoxygenase. The help of artificial intelligence was essential in this study and the results indicate once more that machine learning will be a leading tool for drug discovery in the future. Congratulations to Tiago and all our co-workers that participated in this study! Check out the highlight and the paper.

June 2018

Congratulations to Gonçalo who was appointed as a University Lecturer at the Department of Chemistry, University of Cambridge after 5 years as a Royal Society URF! Great news!

ABOUT OUR WORK

about our work

Nature has produced an intricate machinery to covalently diversify the structure of proteins after their synthesis in the ribosome. At the core of our research and in an attempt to mimic nature, we are engineering reactions that allow for post-expression modification of proteins at selected sites. We use such reactions to selectively install particular modifications on proteins for many biological and therapeutic applications. For example, we are developing strategies for site-selective protein labelling in live cells by combining the introduction of small-sized non-proteinogenic tagged amino acids with very rapid chemoselective reactions. We aim to apply these to label and monitor disease-associated proteins under native conditions without interfere with the protein’s innate structure, function, activity and localisation as well as cellular functions.
Another important aspect of protein modification is for example the conjugation of cytotoxic molecules to antibodies to improve efficacy and reduce side effects of cancer treatments. Gonçalo’s laboratory is engineering new reactions that can be performed site-selectively on native antibodies, i.e. without the need for sequence engineering.
These are two examples among other lines of research in our lab that have in common the use of synthetic aqueous chemistry to address challenges in biology and medicine. Our ultimate goal is to see the widespread use of our findings and methodologies by other laboratories around the world and to directly assist in the design and discovery of new drugs with improved selectivity and efficacy for treating cancer.

ABOUT OUR WORK

about our work

Nature has produced an intricate machinery to covalently diversify the structure of proteins after their synthesis in the ribosome. At the core of our research and in an attempt to mimic nature, we are engineering reactions that allow for post-expression modification of proteins at selected sites. We use such reactions to selectively install particular modifications on proteins for many biological and therapeutic applications. For example, we are developing strategies for site-selective protein labelling in live cells by combining the introduction of small-sized non-proteinogenic tagged amino acids with very rapid chemoselective reactions. We aim to apply these to label and monitor disease-associated proteins under native conditions without interfere with the protein’s innate structure, function, activity and localisation as well as cellular functions.
Another important aspect of protein modification is for example the conjugation of cytotoxic molecules to antibodies to improve efficacy and reduce side effects of cancer treatments. Gonçalo’s laboratory is engineering new reactions that can be performed site-selectively on native antibodies, i.e. without the need for sequence engineering.
These are two examples among other lines of research in our lab that have in common the use of synthetic aqueous chemistry to address challenges in biology and medicine. Our ultimate goal is to see the widespread use of our findings and methodologies by other laboratories around the world and to directly assist in the design and discovery of new drugs with improved selectivity and efficacy for treating cancer.

University of Cambridge
Department of Chemistry
Lensfield Road, Cambridge CB2 1EW, UK
Tel: +44 (0) 1223336305
gb453@cam.ac.uk

Instituto de Medicina Molecular
Faculdade de Medicina da Universidade de Lisboa
Av. Prof. Egas Moniz - 1649-028 Lisboa
Portugal
gbernardes@medicina.ulisboa.pt

University of Cambridge
Department of Chemistry

Lensfield Road, Cambridge CB2 1EW, UK

Tel: +44 (0) 1223336305
gb453@cam.ac.uk

Instituto de Medicina Molecular
Faculdade de Medicina da Universidade de Lisboa

Av. Prof. Egas Moniz - 1649-028 Lisboa
Portugal

gbernardes@medicina.ulisboa.pt