Transfidelity
← Transfidelity

Scientific overview

Raising decoding accuracy to keep proteins folding right

Transfidelity’s small molecules act upstream of aggregation — at the ribosome itself — increasing the fidelity of codon reading so that aging neurons make fewer misfolded proteins.

Draft overview — placeholder copy and figures, pending scientific review

A researcher pipetting samples into tubes at a laboratory bench

Mechanism

From mistranslation to neurodegeneration

  1. 01

    Ribosomes lose accuracy with age

    In aging neurons, the ribosome makes more decoding errors — misreading codons and reading through stop signals.

  2. 02

    Errors produce aberrant proteins

    Each mistranslation event yields a protein with the wrong sequence, more prone to misfolding than its faithful counterpart.

  3. 03

    Quality control is overwhelmed

    A rising load of aberrant proteins saturates chaperones and degradation pathways, tipping the cell into proteostatic stress.

  4. 04

    Aggregates drive degeneration

    Misfolded proteins aggregate — including α-synuclein and amyloid species — and neurons progressively fail.

Pipeline

Where the program stands

Target & discovery

Established

Hit-to-lead

In progress

Preclinical — Parkinson’s

Active

IND-enabling

Planned

Supporting figures

Data behind the approach

Final figures will be supplied by the team. The placeholders below show the intended structure and captions.

Fig. 1 · placeholder
Stop-codon readthrough reduced ~20–25% in mammalian cells by lead compounds.
Fig. 2 · placeholder
Proteostasis-sensor readouts improve across HEK293 and neuronal models.
Fig. 3 · placeholder
α-synuclein aggregates decrease in iPSC-derived 3× SNCA patient neurons.
Fig. 4 · placeholder
No detectable global translation inhibition at active concentrations.

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