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Event date and time

Wednesday 14 Apr 2021
12.00 noon AEST (Brisbane time)


Online virtual event
Webinar login details will be emailed to registrants

We are delighted to bring you the next virtual Synthetic Biology Future Science Platform Seminar Series. This will be an opportunity for you to hear, in detail, each month about the latest work from SynBioFSP funded projects, CSIRO-University Fellows and SynBioFSP PhD students.


  • Free

Dates and Times

Event date: Apr 2021

Wednesday 14 Apr 2021

Online virtual event

12.00 noon AEST (Brisbane time)

Webinar login details will be emailed to registrants

Booking closed



More information

Seminar Program:

Welcome, Acknowledgement of Traditional Owners and introduction of speakers by Dr Colin Scott, Application Domain Leader, Foundation Technologies

Title: A dual glycoengineering system; the prospects of a multi-avenue approach to targeted glycoprotein production

Nicholas DeBono

Speaker #1: Nicholas DeBono, Macquarie University and CSIRO Synthetic Biology Future Science Platform

Bio: Nicholas completed a Bachelor of Advanced Science in Biomolecular Sciences at Macquarie University in 2018, during which his interest in Synthetic Biology and Biochemistry grew. This led to a Master of Research thesis titled “A dual glycoengineering system: combining synthetic biology with an Artificial Golgi Column”, work that he has continued into his current PhD undertaking. His research focusses on the potentials of glycoengineering, and he is interested in finding and investigating intersections within molecular science fields.

Abstract: When a glycoengineered high-yield producing yeast is coupled to an in vitro glycosylating column, a scalable, glycan-defined glycoprotein production system can be created. This dual glycoprotein production system has several potential applications and could be beneficial for creating glycan-defined glycoproteins with targeted structures. Building on previous work, we are working to create a scalable workflow to produce glycoproteins with targeted glycoforms that may be of interest in an academic and therapeutic sense. This workflow is planned to incorporate the widely used methylotrophic yeast, Pichia pastoris and an Artificial Golgi Column, and will be designed to be suitable for multiple glycoproteins.

Title: Design of switchable protein interfaces: harnessing post-translational modifications for synthetic biology

Dr Daniel Winter

Speaker #2: Dr Daniel Winter, University of New South Wales and CSIRO Synthetic Biology Future Science Platform Fellow

Bio: Native of Rio de Janeiro, Daniel moved to Paris in 2007 where he obtained his Bachelor's and Master's degrees in Biochemistry and in Protein Engineering at the Université Paris Diderot. As fate would have it, an exchange semester in 2013 at the University of New South Wales turned into a very prolonged stay in Sydney. At UNSW, Daniel obtained a scholarship to join Prof. Marc Wilkins' group for his PhD, during which time he authored and co-authored a series of papers on the systems biology and analytical mass spectrometry of protein interactions and their post-translational modifications (PTMs). Alongside his PhD, Daniel mentored the first iGEM teams from UNSW and made his initial forays into synthetic biology. Following his doctoral research, Daniel joined Dr Dominic Glover's group at UNSW as the recipient of a CSIRO Synthetic Biology Future Science Fellowship, where he is applying his expertise in protein interactions and PTMs to design novel, enzyme-responsive protein modules for smart biomaterials and orthogonal signalling pathways.

Abstract: The design of protein interaction interfaces is a cornerstone of synthetic biology, where they can be used to promote the association of protein subunits into active molecular complexes or into protein nanostructures. In nature, protein interactions are modulated by enzymatic post-translational modifications (PTMs) that modify the protein interfaces with various chemical groups. PTMs thus represent a means to gain control over protein interactions. Yet, they have seldom been considered in the design of synthetic proteins. We are exploring the potential of a reversible PTM, serine phosphorylation, to modulate the interactions between peptides. Using the well-established dimeric coiled coil interaction as a template, we have rationally designed a series of interacting peptide pairs whose binding affinities are regulated by the activity of protein kinase A. Such kinase-regulated peptide interfaces can be appended to proteins of interest to enzymatically control their interactions. Our next objective is to increase the throughput when designing kinase-regulated peptide interfaces. For this purpose, we have developed a computational strategy where molecular dynamics simulations are used to predict changes in binding affinity upon phosphorylation of target serine residues. De novo designed PTM-modulated interfaces will be useful to control the association of proteins in biological circuits and smart nanostructures.

Upcoming Events:

Future events in this series are planned for the following dates and times:

Please note that this seminar will be recorded.

Please direct any seminar series enquiries to