bioRxiv Science⌕ Search

Biology subjects

Kwan, T. O. C.

Publications and source records attributed to Kwan, T. O. C..

2 recordsLinked to original sources

Designing enzymes for new-to-nature chemistry and non-natural substrates with AlphaProtein Novo

Creating highly active enzymes for arbitrary reactions is a transformative goal for the molecular sciences (1). Traditional protein engineering (2,3) is constrained by a reliance on existing natural starting points, which are often challenging to discover. De novo design offers the potential to overcome this by creating enzymes from first principles (4), but has yet to achieve practically relevant catalytic properties. Here we present AlphaProtein Novo (AP Novo), a machine-learning pipeline that demonstrates, for the first time, that de novo enzyme design can outperform natural sequence mining in addressing challenging chemistry. We used AP Novo to design new-to-nature nitrene transferases to synthesise the pharmacophore piperidine with unprecedented product selectivity, and to create enzymes that degrade the environmental toxin DEHP under conditions that denature natural enzymes. We also obtained state-of-the-art catalytic efficiencies on two well-studied model reactions, and through iterative design and analysis found that key enablers of success were mechanism-inspired metrics based on AlphaFold 3 predictions and sequence-ensemble-based scoring of designed backbones. Our results show that de novo design has become a powerful complement to natural enzyme diversity for discovering catalysts for a range of applications.

synthetic biology↗

Spontaneous oligomerization of BAK/BAX is suppressed by hetero-dimerization with MCL-1

BCL-2 proteins control the intrinsic pathway of programmed cell death. Composed of anti- and pro-apoptotic members, their network of interactions forms a molecular switch that controls mitochondrial outer-membrane permeability. Apoptotic stimulation leads to BAK/BAX oligomerization and pore formation, yet the molecular details of this pivotal step remain poorly understood, and controversy persists regarding the activation mechanism. Here we use native mass spectrometry and kinetics to show that the homo-oligomerization of BAK and BAX is spontaneous in hydrophobic environments. This process is abrogated by hetero-dimerization of both BAK and BAX with the anti-apoptotic BCL-2 protein MCL-1. Pro-apoptotic BH3-only proteins disrupt these hetero-dimers by binding competitively to MCL-1, releasing BAK/BAX for homo-oligomerization. Thus, we infer that their oligomeric states are thermodynamically favored at the membrane. Our approach provides the framework for future quantitative biophysical characterizations of the BCL-2 network, and advances our molecular understanding of apoptosis.

biophysics↗