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Ogden, P.

Publications and source records attributed to Ogden, P..

3 recordsLinked to original sources

Latent generative search unlocks de novo design of untapped biomolecular interactions at scale

De novo protein design has advanced rapidly, yet designing binders to polar, solvent-exposed epitopes and small, flexible ligands remains challenging. Such hydrated surfaces and flexible molecules, including carbohydrates, provide few of the hydrophobic contacts favoured by current methods and have largely resisted de novo binders. To address this challenge, here we introduce latent generative search for binder design, a novel framework that uses reward-guided search at inference time to steer the Proteina-Complexa generative model. The model codesigns sequence and structure - generating them together in a continuous latent space - and thereby removes the inverse-folding step on which current methods rely. In a screen of more than one million designs by multiplexed phage display, latent generative search produced more validated binders than every other method tested, its codesigned sequences surpassing post hoc redesign. It delivered high-affinity binders across therapeutic receptors, a viral attachment protein and intracellular signalling targets. Our approach also accessed previously untapped biology, generating the first de novo proteins that bind a free carbohydrate, including one that discriminates between blood-group antigens - a polar, flexible target class beyond the reach of current design methods.

bioengineering↗

mBER: Controllable de novo antibody design with million-scale experimental screening

AO_SCPLOWBSTRACTC_SCPLOWRecent machine learning approaches have achieved high success rates in designing protein binders that demonstrate in vitro binding to their targets. While open models for unconstrained "minibinder" design have shown great experimental promise, methods for designing binders in specific formats, such as antibodies, have lagged behind in experimental success rates. In this work, we present mBER, an open-source protein binder design system capable of designing antibody-format binders with state-of-the-art experimental success rates. mBER builds on the ColabDesign framework, achieving successful antibody design primarily through the inclusion of informative sequence and structure conditioning information. Using mBER, we designed two libraries comprising over 1 million VHH binders against 436 diverse targets. We experimentally screened the two libraries against 145 of these targets, resulting in a dataset of over 100 million binding interactions. We achieved specific and significant design success against 45% of targets. In a filtered set of designs, we detect binding rates to specific epitopes as high as 38%. Through mBER, we demonstrate that format-specific binder design is possible with no additional training of underlying folding and language models. This work represents the largest reported de novo protein design and validation campaign, and one of the first open-source methods to demonstrate double-digit percentage experimental success rates for antibody binder design.

synthetic biology↗

A Liquid Chromatography-Mass Spectrometry Method For Screening Disulfide Tethering Fragments

We report the refinement of a high-throughput, liquid-chromatography/mass spectrometry (LC/MS)-based screening method for the identification of covalent small-molecule binders to proteins. Using a custom library of 1600 disulfide-capped fragments targeting surface cysteine residues, we optimize sample preparation, chromatography, and ionization conditions to maximize the reliability and flexibility of the approach. Data collection at a rate of 90 seconds per sample balances speed and reliability for sustained screening over multiple, diverse projects run over a 24-month period. The method is applicable to protein targets of various classes and a range of molecular masses. Data are processed in a custom pipeline that calculates a % bound value for each compound and detects false-positives by calculating significance of detected masses ( signal significance). An example pipeline has been made available through Biovias ScienceCloud Protocol Exchange. Data collection and analysis methods for the screening of covalent adducts of intact proteins are now fast enough to screen the largest covalent compound libraries in 1-2 days.

biophysics↗