Negative Results Bundle 😅 We just published 3 new collections on Proteinbase, and they're mostly negative results: · Boolean Biotech's (@btnaughton) VHH Competition (6 VHHs vs MBP) · @EvolvedTechInc Hackathon (80 designs vs CD16a/CD16-2) · PD-L1 FoldCraft by @KhRRustamov (35 de novo vs PD-L1) Clean non-binder data is still quite rare and useful, especially for training models. All open under ODC-ODbL.

🧬 We picked the 300 designs going to the wet-lab for the @gembioworkshop x @adaptyvbio RBX1 Binder Design Competition. 12000 submissions from 180 designers. About 6x the volume we had expected. Expression and binding affinity measurements are now running. Results will be presented at the @gembioworkshop workshop at @iclr_conf 2026 in Rio 🇧🇷

🚨 𝗙𝗜𝗡𝗔𝗟 𝗛𝗢𝗨𝗥𝗦: @gembioworkshop 𝘅 @Adaptyv 𝗥𝗕𝗫𝟭 𝗕𝗶𝗻𝗱𝗲𝗿 𝗗𝗲𝘀𝗶𝗴𝗻 𝗖𝗼𝗺𝗽𝗲𝘁𝗶𝘁𝗶𝗼𝗻 - 𝗦𝘂𝗯𝗺𝗶𝘀𝘀𝗶𝗼𝗻𝘀 𝗰𝗹𝗼𝘀𝗲 𝘁𝗼𝗻𝗶𝗴𝗵𝘁! 🚨 Submissions for the RBX1 protein binder design competition close tonight at 00:59 CET (March 27). Quick recap: Design protein binders against RBX1, a cancer-relevant E3 ligase subunit. Half disordered, RING domain with zinc ions, making it a real design challenge. 300 designs will be experimentally tested in the @Adaptyv lab. Results at @iclr_conf 2026 in Rio. Open to everyone.

Submissions are open for the GEM x @adaptyvbio RBX1 Binder Design Competition 🧬 We're partnering with the GEM Workshop at ICLR 2026 for a new protein design challenge. The target is RBX1, a 108-amino acid component of Cullin-RING E3 ubiquitin ligase complexes, which control degradation of roughly 20% of all cellular proteins. In many cancers, this protein is overexpressed and degrades important tumor suppressing proteins. Disrupting RBX1's function with a de novo designed binder could slow down cancer cell proliferation. But RBX1 is a tricky design problem. Half the protein is an intrinsically disordered N-terminus so it has limited use for structure-based design methods. The part you actually need to bind, the E2 recruitment surface on helix α2, sits within a RING domain with an usual fold that is shaped by three coordinated zinc ions. How it works: - Submit up to 100 ranked binder sequences (≤250 aa) with a design method description on Proteinbase till March 26 - An expert panel from the GEM workshop selects 300 designs based on novelty and originality - We test all 300 for expression and binding affinity in the @Adaptyv Bio lab - Experimental results will be released April 26 at ICRL 2026 in Rio de Janeiro and open-sourced on Proteinbase Prizes: $1,000 for the best binder, $100 for the runner-up, and co-authorship on the results paper.

Announcing the winners of the “De Novo” track of the Nipah Protein Design Competition! This track rewards completely novel design ideas. No starting scaffold, no antibody to optimize, no template to tweak: just the target structure and a blank canvas. Winners (by best binding strength) 🥇 Nick Boyd (Escalante) — KD: 1.4e-9 M 🥈 Johannes Klier (Schoeder lab)— KD: 1.2e-8 M 🥉 Brian Coventry (@UWproteindesign) — KD: 1.8e-8 M

Nipah virus protein design competition update: The lab has been running nonstop for two weeks validating all 1,200 selected proteins. We’re now finalizing the last assays to make sure everything is properly validated, so we’re moving the results release to Wednesday, January 21st at 9am PST / 6pm CET. One thing we can say now: there are binders! 👀

Also, last chance to make your predictions about the results on @ManifoldMarkets : manifold.markets/Proteinbase…

Nipah virus protein design competition update: The lab has been running nonstop for two weeks validating all 1,200 selected proteins. We’re now finalizing the last assays to make sure everything is properly validated, so we’re moving the results release to Wednesday, January 21st at 9am PST / 6pm CET. One thing we can say now: there are binders! 👀