Danny D. Sahtoe

This study designs de novo proteins that selectively inhibit alpha-synuclein aggregation by targeting specific intermediates, with one binder preferentially inhibiting oligomer formation and secondary nucleation.

This paper presents a modular strategy to design programmable, highly porous protein crystals with tunable architectures and composition, enabling applications in catalysis and biomedicine.

The paper designs proteins with controlled dissociation rates by introducing strained excited states, enabling rapid cytokine receptor dissociation.

The paper identifies a cellular tipping point between aggregate accumulation and removal as a universal feature of neurodegeneration, validated through live-cell assays and super-resolution imaging.

The paper designs peptide traps that bind amyloidogenic segments in {beta}-strand and {beta}-hairpin conformations, effectively blocking fibril assembly for A{beta}42.

This paper designs reconfigurable asymmetric protein assemblies using implicit negative design principles, enabling stable subunit exchange and diverse complex formations.

The paper introduces a computational method for designing rigid protein assemblies through three-body fusion and validates it experimentally with mass spectrometry and cryo-EM.