I've had that last one deleted and re-posted here, minus the 2nd...

I've had that last one deleted and re-posted here, minus the 2nd presentation. I'm not able to verify my comments about links to that research.  
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In the report PYC mention the work with IMB:
... in the ARC grant-funded collaboration with the Institute for Molecular Biosciences at University of Queensland, high hit rates have been confirmed from new synthetic Phylomer libraries against several target classes. This collaboration is on track for the validating of prototype arrays of Phylomers for use in universal diagnostics.

At the Lorne Conference (5-9Feb2017) the following presentation (108 on page54) was on this work. Notice the lead investigators Akshay Bhumkar and Yann Gambin, are from 'Single Molecule Sciences, EMBL Node, Uni of NSW.

Small peptide molecules: novel therapeutics and biomarkers
Akshay Bhumkar1 , Mehdi Moustaqil1 , Nadia Milech2 , Heique Bogdawa2 , Ailis O'Carroll1 , Nichole Giles1 , Dominic Hunter3 , Wayne Johnston3 , Kirill Alexandrov3 , Emma Sierecki1 , Paul Watt4 , Yann Gambin1
1. Single Molecule Sciences, EMBL Node, UNSW, Randwick, NSW, Australia
2. Telethon Kids Institute, Perth, WA, Australia
3. Institute for Molecular Bioscience, St. Lucia, QLD, Australia
4. Phylogica Ltd, Perth, WA, Australia

Recent advances in therapeutic research have led to an increasing number of small peptides being used as drug like molecules that are highly specific and which offer greater efficacy while being safe for human consumption(Fosgerau and Hoffmann 2015). Metabolic diseases and oncology form a major fraction of therapeutic targets for peptides, with peptides being studied as an alternative to chemotherapy(Kaspar and Reichert 2013). Here we discuss a high throughput assay established to screen a peptide library (Phylomers) for target – peptide interactions and to test their efficacy as protein – protein interaction disruptors.
For our study, library of 10000 Phylomers was generated based on a limited repertoire of protein interaction motifs found in nature that exhibit high affinity interactions and bioactivity, from which 384 were selected (encompassing variety of structural folds with differential degree of net charge and hydrophobicity - hydrophilicity) for our initial study. The phylomers were cloned in gateway vectors with a C- terminal cherry-myc tag for expression in the Leishmania tarentolae cell-free system. Our assay identified six phylomers that have high specificity and efficacy towards cMyc and SOX18, important genes which are associated with cancer metastasis. These phylomers bind tightly to the targets and 3/10 phylomers disrupt cMyc and SOX18 interaction with their respective partners with low-micromolar affinity. These phylomers are currently been tested in an in-vivo assay to study their efficacy in cells. If successful these phylomers can form the newest breed of small peptide drug-like molecules
Our phylomer screen is currently being expanded to assess the capacity of phylomers to specifically detect mutated / oligomeric state of proteins associated with diseases and disorders. The specific phylomers can form the basis of novel biomarkers that can selectively detect genomic mutations associated with diseases and can be developed as early detection kits for certain genetic illnesses.

http://www.lorneproteins.org/assets/Proteins-E-BOOK-Sunday-05022017.pdf
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