Our presenters in the next RSC Peptide and Protein Science Group online seminars will be Dr Chiara Maniaci from Dundee and Simon Tang from Bath.
Date: 05-07-2024
Time: 1:00-2:00 pm
Venue: an online Zoom lecture
Registration: https://eu01web.zoom.us/meeting/register/u5Uud-2gpj8iEtIWyX5fA88VRFYXXkiTibHt
Dr Chiara Maniaci
Title: 鈥淐leave to Modify鈥�: A new biological mechanism for protein regulation
It is well understood that the complexity of cellular proteome derives in large part from changes beyond transcription and translation. One way the cell diversifies its proteome is by using proteases to post-translationally cleave progenitor proteins. The released neo-protein fragments may be stable in vivo and acquire neo-functions of biological and therapeutic relevance. I have recently discovered that the neo-proteins, in particular their newly revealed neo-termini, become hotspots for post-translational modifications, a mechanism I refer to as 鈥渃leave to modify鈥�. The revealed 鈥渃leave-to-modify鈥� mechanism exemplifies a concept that may be general and widespread, opening exciting avenues to discover new biology and tools. This seminar will highlight our latest effort in elucidating the molecular mechanism underpinning these unprecedented post-translational modification events.
Dr Simon Tang
Title: A Bio-Based Solution to Sustainable Cyclic Peptide Production and Drug Discovery: Intracellular Peptide Cyclisation by an Asparaginyl Endopeptidase
Cyclic peptides are a privileged class of drug molecules increasingly offering access to the 85% of the proteome which is yet to be drugged. However, cyclic peptide synthesis is challenging; existing methods employ toxic and unsustainable reagents, presenting a bottleneck that restricts drug discovery.
In this talk, I will give an overview of my research towards the use of an asparaginyl endopeptidase for peptide ligation and cyclisation, showcasing its application during recombinant expression in E. coli to enable concomitant in situ cyclisation, which I anticipate having broad utility in a range of biochemical and chemical applications.
Date: 05-07-2024
Time: 1:00-2:00 pm
Venue: an online Zoom lecture
Registration: https://eu01web.zoom.us/meeting/register/u5Uud-2gpj8iEtIWyX5fA88VRFYXXkiTibHt
Dr Chiara Maniaci
Title: 鈥淐leave to Modify鈥�: A new biological mechanism for protein regulation
It is well understood that the complexity of cellular proteome derives in large part from changes beyond transcription and translation. One way the cell diversifies its proteome is by using proteases to post-translationally cleave progenitor proteins. The released neo-protein fragments may be stable in vivo and acquire neo-functions of biological and therapeutic relevance. I have recently discovered that the neo-proteins, in particular their newly revealed neo-termini, become hotspots for post-translational modifications, a mechanism I refer to as 鈥渃leave to modify鈥�. The revealed 鈥渃leave-to-modify鈥� mechanism exemplifies a concept that may be general and widespread, opening exciting avenues to discover new biology and tools. This seminar will highlight our latest effort in elucidating the molecular mechanism underpinning these unprecedented post-translational modification events.
Dr Simon Tang
Title: A Bio-Based Solution to Sustainable Cyclic Peptide Production and Drug Discovery: Intracellular Peptide Cyclisation by an Asparaginyl Endopeptidase
Cyclic peptides are a privileged class of drug molecules increasingly offering access to the 85% of the proteome which is yet to be drugged. However, cyclic peptide synthesis is challenging; existing methods employ toxic and unsustainable reagents, presenting a bottleneck that restricts drug discovery.
In this talk, I will give an overview of my research towards the use of an asparaginyl endopeptidase for peptide ligation and cyclisation, showcasing its application during recombinant expression in E. coli to enable concomitant in situ cyclisation, which I anticipate having broad utility in a range of biochemical and chemical applications.
