The next early career academics presenting in the Peptide and Protein Science online series will be Dr Andrew Beekman from the University of East Anglia and Dr Chris Waudby from University College London.
Date: 3-11-2023
Time: 1:00-2:00 pm
Venue: an online Zoom lecture
Registration: https://eu01web.zoom.us/meeting/register/u5csceCgrzorGNWQVPASJQQTUMHOQFSuWSWT
Dr Andrew Beekman - University of East Anglia
Title: Taking inspiration from disease to modulate protein-protein interactions in cancer
Abstract: Aberrant protein-protein interactions (PPIs) result in, and control, several of the hallmarks of cancer. PPIs can be controlled by peptides, but there are hundreds of thousands of PPIs, making selecting an appropriate target a challenging task. Our approach is to look to disease for inspiration. PPIs which are exploited by cancer are often aberrant in other disease states. For example, telomerase, the protein complex responsible for extending telomeres on the ends of DNA and allowing continued replication, is exploited by cancer to allow replicative immortality. In early-ageing diseases this protein complex is deficient. We design and synthesise peptide analogues to help control these PPIs in cancer.
Dr Chris Waudby - University College London
Title: Investigating glycoprotein misfolding and quality control using NMR
Abstract: Approximately one third of eukaryotic proteins are translocated co-translationally into the endoplasmic reticulum for processing prior to secretion. Within the ER, N-linked glycosylation of the nascent polypeptide defines a ‘glycan code’ that regulates its engagement with components of the glycan quality control (GQC) pathway. Failure of GQC can result in protein misfolding, accumulation in the ER, and the onset of disease. Within the Waudby group, we are developing strategies to study the misfolding of glycoproteins using multinuclear, ex vivo NMR, coupled with single molecular biophysical methods, and to study the structural basis of recognition of misfolded glycoproteins by components of the GQC pathway.
For upcoming series, please visit the UUÂãÁÄÖ±²¥ PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: louise.walport@crick.ac.uk
Date: 3-11-2023
Time: 1:00-2:00 pm
Venue: an online Zoom lecture
Registration: https://eu01web.zoom.us/meeting/register/u5csceCgrzorGNWQVPASJQQTUMHOQFSuWSWT
Dr Andrew Beekman - University of East Anglia
Title: Taking inspiration from disease to modulate protein-protein interactions in cancer
Abstract: Aberrant protein-protein interactions (PPIs) result in, and control, several of the hallmarks of cancer. PPIs can be controlled by peptides, but there are hundreds of thousands of PPIs, making selecting an appropriate target a challenging task. Our approach is to look to disease for inspiration. PPIs which are exploited by cancer are often aberrant in other disease states. For example, telomerase, the protein complex responsible for extending telomeres on the ends of DNA and allowing continued replication, is exploited by cancer to allow replicative immortality. In early-ageing diseases this protein complex is deficient. We design and synthesise peptide analogues to help control these PPIs in cancer.
Dr Chris Waudby - University College London
Title: Investigating glycoprotein misfolding and quality control using NMR
Abstract: Approximately one third of eukaryotic proteins are translocated co-translationally into the endoplasmic reticulum for processing prior to secretion. Within the ER, N-linked glycosylation of the nascent polypeptide defines a ‘glycan code’ that regulates its engagement with components of the glycan quality control (GQC) pathway. Failure of GQC can result in protein misfolding, accumulation in the ER, and the onset of disease. Within the Waudby group, we are developing strategies to study the misfolding of glycoproteins using multinuclear, ex vivo NMR, coupled with single molecular biophysical methods, and to study the structural basis of recognition of misfolded glycoproteins by components of the GQC pathway.
For upcoming series, please visit the UUÂãÁÄÖ±²¥ PPSG website.
If you would like to present in future seminars, please contact one of the organisers.
Louis Luk: lukly@cardiff.ac.uk
Chris Coxon: chris.coxon@ed.ac.uk
Louise Walport: louise.walport@crick.ac.uk
