Amy Weeks

@amyweeks.bsky.social

Asst Prof @ UW-Madison Biochemistry. Protein Engineering, Chemical Biology, Proteomics, Proteases, Enzymology.

A bit late but…Tenured! Immense gratitude for those who got us here. Firstly the students/postdocs (too many to list!) who took a chance on an unproven lab and were unafraid to pursue some strange new ideas. I couldn't have predicted our path, and I couldn’t be more excited for what's next.

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@zjmaggiexu.bsky.social's story on suctorian trap structure adaptation is now online in @currentbiology.bsky.social , with new evolutionary analyses and modeling! This fall, Maggie will keep exploring predatory protists as a PD in @nbellono.bsky.social group; keep an eye out for her she's amazing!

sciencedirect.com

Scott Coyle@cellraiser.bsky.social · 9mo ago

How do cells adapt morphology to function? In a 🔥 preprint by @zjmaggiexu.bsky.social , with @dudinlab.bsky.social and @amyweeks.bsky.social , we identify a self-organizing single-cell morphology circuit that optimizes the feeding trap structure of the suctorian P. collini. 🧵 tinyurl.com/4k8nv926

Excited to share our new bioRxiv preprint! We introduce RIPPLE, a synthetic platform that couples reaction–diffusion signaling with protein condensation to generate tunable intracellular architectures. Grateful to @zjmaggiexu.bsky.social and @cellraiser.bsky.social. It’s been a rewarding journey.

Scott Coyle@cellraiser.bsky.social · 2mo ago

Sub-cellular architectures arise through integrating signaling and structure. @edenchang.bsky.social and @zjmaggiexu.bsky.social show how coupling reaction-diffusion signaling to protein condensation provides a tunable, regulatable landscape for sub-cellular structure www.biorxiv.org/content/10.6...

Now online @pnas.org: We developed a simple, scalable, and accessible platform for deep profiling of phosphoeraser specificity using human phosphoproteome-derived peptide libraries (PhosPropels!) 🧪👩‍🔬https://www.pnas.org/doi/10.1073/pnas.2523183123

Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases | PNAS

Protein phosphorylation is dynamically regulated by the opposing activities of phosphowriter enzymes (kinases) and phosphoeraser enzymes (phosphata...

pnas.org

Thanks to the Ono Pharma Foundation and The University of Chicago for supporting this amazing symposium! And congratulations to the Weeks lab's own Sopo Jalalishvili for winning a poster prize for her work on phospholyases! 👩‍🔬🧪@uwbiochem.bsky.social

ONO PHARMA FOUNDATION@onoinitiative.bsky.social · 2mo ago

Great momentum at 2026 Chicago Chemical Biology and Therapeutics Symposium, hosted by CCBT at The University of Chicago and Ono Pharma Foundation. Insightful presentations and meaningful interactions drove the success of the meeting. Grateful to all attendees! ccbt.bsd.uchicago.edu/events/

Excited to share our lab's latest preprint, led by graduate student Minhee Lee, with contributions from former undergrad Zijing Wang and grad student Andrew Johns! We show that substrate specificity information coupled with AF3 models can be used to design selective tyrosine kinase inhibitors.

bioRxiv Biochemistry@biorxiv-biochem.bsky.social · 3mo ago

Substrate-derived peptides for selective covalent inhibition of protein tyrosine kinases https://www.biorxiv.org/content/10.64898/2026.05.11.724146v1

Excited that our paper on enzymatic bromination of peptides is now online at ACS Chemical Biology! Led by Haley Bridge, we showed that the flavin-dependent halogenase RebH and its variants can be used for late-stage chemoenzymatic diversification of bioactive peptides: pubs.acs.org/doi/10.1021/...

Enzymatic Bromination of Native Peptides for Late-Stage Structural Diversification via Suzuki–Miyaura Coupling

Flavin-dependent halogenases (FDHs) provide a biocatalytic approach for the site-selective halogenation of aromatic compounds, but their use in late-stage functionalization of peptides has remained li...

pubs.acs.org

🚨 excited to share our latest preprint on bioRxiv, led by the soon-to-be Dr. Guy Kunzmann! We tackle a striking case of conditional dependence on UFMylation, a UBL modification pathway whose contributions to cell fitness have been a bit of a "black box." 🧵

bioRxiv Cell Biology@biorxiv-cellbio.bsky.social · 4mo ago

Dynamic UFMylation governs cellular fitness by coordinating multi-organelle proteostasis https://www.biorxiv.org/content/10.64898/2026.03.27.714830v1

New preprint! We found that the flavin-dependent halogenase RebH catalyzes sequence-tolerant Trp bromination in peptides 🧪https://www.biorxiv.org/content/10.64898/2025.12.17.694899v1

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Thrilled to share our work on the 🔥 single-celled predator Podophrya collini, which rewires its cell morphology to hunt more efficiently. Huge thanks to our amazing team—Amy, Lauren, Omaya, Marine, Mari, and especially Scott—for making this shine! ✨

Scott Coyle@cellraiser.bsky.social · 9mo ago

How do cells adapt morphology to function? In a 🔥 preprint by @zjmaggiexu.bsky.social , with @dudinlab.bsky.social and @amyweeks.bsky.social , we identify a self-organizing single-cell morphology circuit that optimizes the feeding trap structure of the suctorian P. collini. 🧵 tinyurl.com/4k8nv926

Excited to share our new preprint, which was years in the making! chemrxiv.org/engage/chemr... New reactions are typically developed by trial and error. How can we speed up this process? Read on to learn how we used DNA scaffolding to perform >500,000 parallel reactions on attomole scale. 1/n

DNA-Scaffolded Ultrahigh-Throughput Reaction Screening

Discovering and optimizing reactions is central to synthetic chemistry. However, chemical reactions are traditionally screened using relatively low-throughput methods, prohibiting exploration of diver...

chemrxiv.org

Check out our new manuscript on parallel LC separations! Super cool how the very high scan rates of modern MS systems coupled with DIA can allow us to run several samples at the same time with little loss in depth. Congrats to Noah and the team. #JASMS pubs.acs.org/doi/10.1021/...

SynchroSep-MS: Parallel LC Separations for Multiplexed Proteomics

Achieving high throughput remains a challenge in MS-based proteomics for large-scale applications. We introduce SynchroSep-MS, a novel method for parallelized, label-free proteome analysis that leverages the rapid acquisition speed of modern mass spectrometers. This approach employs multiple liquid chromatography columns, each with an independent sample, simultaneously introduced into a single mass spectrometer inlet. A precisely controlled retention time offset between sample injections creates distinct elution profiles, facilitating unambiguous analyte assignment. We modified the DIA-NN workflow to effectively process these unique parallelized data, accounting for retention time offsets. Using a dual-column setup with mouse brain peptides, SynchroSep-MS detected approximately 16,700 unique protein groups, nearly doubling the peptide information obtained from a conventional single proteome analysis. The method demonstrated excellent precision and reproducibility (median protein %RSDs less than 4%) and high quantitative linearity (median R2 greater than 0.96) with minimal matrix interference. SynchroSep-MS represents a new paradigm for data collection and the first example of label-free multiplexed proteome analysis via parallel LC separations, offering a direct strategy to accelerate throughput for demanding applications such as large-scale clinical cohorts and single-cell analyses without compromising peak capacity or causing ionization suppression.

pubs.acs.org

Excited to share our latest: we engineered the reactivity of a bacterial E1-like enzyme for ATP-driven modification of C termini. Our tool mimics the logic of peptide bond formation in biology for precision modification of proteins in vitro. 🧪https://rdcu.be/ewN7C

Engineered reactivity of a bacterial E1-like enzyme enables ATP-driven modification of protein and peptide C termini

Nature Chemistry - In living systems, ATP provides an energetic driving force for protein synthesis and modification. Now, an engineered enzymatic tool has been developed for high-yield, ATP-driven...

rdcu.be

Despite ~20 years in/around #chembio research, I went to my first Bioorganic GRC this week. This community is amazing and so supportive. I feel energized (and tired, lol) and find myself rooting for the next generation of chemical biologists. Sooooo much awesome science - We can’t/won’t be stopped!