+ ONCHAIN CARDIOVASCULAR RESEARCH
The heart of
open science.
Understanding the molecular machinery of the heart.
Building a future where every scientific step
can be independently verified.
TO MOLECULE
OUR MOLECULAR FOCUS
A complex disease.
A precise starting point.
The heart is powered by molecular motors. Understanding how those motors work—and how small molecules alter their activity—opens a precise window into cardiovascular disease.
ORVIA brings that question into open computational research. Our first focus is cardiac myosin in hypertrophic cardiomyopathy, with a long-term goal of making the calculation itself inspectable on-chain.
Meet the first research question ↗Local prototypeA connected 256-contract fixture demonstrates parts of the execution path.
Scientific acceptance openComplete model preparation, sampling and current-source validation remain.
Production aheadNo ORVIA production contract has been deployed to Robinhood Chain.
THE SCIENCE, AT EVERY SCALE
Look closer.
Understand deeper.
A journey from heart muscle to the molecular
motor that generates force.
When heart muscle
becomes too thick.
Hypertrophic cardiomyopathy (HCM) involves abnormal thickening of the heart muscle. In obstructive disease, this can restrict blood flow out of the left ventricle.
The disease reaches down to the sarcomere—the contractile unit of heart muscle. That is where our molecular investigation begins.
Small changes.
Fundamental questions.
One molecular substitution.
A carefully defined comparison.
A calculation open to scrutiny.
A STATE-SPECIFIC MOLECULAR COMPARISON
What can one
carbon change?
Our proposed first experiment compares compound 17 with aficamten: an oxadiazole methyl-to-ethyl substitution within a declared cardiac-myosin model.
The question is a relative binding free energy—not a clinical outcome. The model, molecular state, sampling and uncertainty must all be specified before interpretation.
Read the proposed protocol ↗ΔΔGbind = ΔGcomplex−ΔGsolvent
The same A → B transformation, in two environments.
Negative values favor B within the declared model.
No validated binding-free-energy result is claimed.
THE SCIENTIFIC METHOD
A result is only as strong
as its conditions.
Question & model
Preregister the A → B transformation, receptor state, protonation, cofactors and force-field parameters.
Two environments
Evaluate the same transformation in the myosin complex and in solvent, using a declared alchemical protocol.
Convergence & uncertainty
Inspect equilibration, state overlap, effective sample size and independent repeats before accepting an estimate.
Evidence & limits
Publish methods, diagnostics and uncertainty. An inconclusive result remains part of the scientific record.
Visualization uses experimental coordinates from PDB 9F6C: bovine cardiac myosin, pre-powerstroke state. Simplified representation; not a molecular-dynamics trajectory. Structure & attribution ↗
Every step.
Open to verification.
Our goal is to place molecular inputs, numerical
work and analysis in contracts—so the path
from question to result remains inspectable.
A result begins with
an explicit question.
Register the molecular state, structures, parameters, units and protocol. Make the scientific assumptions visible before a calculation begins.
Architecture in development. A stored result hash alone does not establish that a calculation ran on-chain.
04 / THE PATH FORWARD
Progress is
earned in evidence.
A scientific roadmap is a sequence of questions that must be resolved. Each stage has an explicit acceptance condition.
Inspect the current research status ↗02 NOVEMBER 2026
01Open methods & foundationsAVAILABLE+
Publish the protocol, numerical components and reproducible checks. Retain source and evidence so independent researchers can inspect the assumptions.
Acceptance: traceable source, methods and reference checks.02Integrated molecular engineIN PROGRESS+
Connect retained state, force calculations, constrained or unconstrained sampling and analysis. A local fixture demonstrates parts of this path; complete current-source validation remains open.
Acceptance: full source-bound validation, including integration failures and recovery.03Prepared system & samplingREQUIRED+
Resolve receptor preparation and complete compatible protein, ligand and cofactor parameters. Establish equilibration, overlap, correlation and repeat uncertainty.
Acceptance: a physically declared model and validated sampling diagnostics.04Full-model chain feasibilityREQUIRED+
Rehearse the complete calculation on the target execution rules. Measure total cost, state growth, numerical agreement and practical throughput.
Acceptance: target-chain evidence for a complete prepared workload.05Independent review & releasePLANNED+
Invite independent scientific and software review. A production release follows only after scientific, computational and operational criteria are met.
Acceptance: reviewable evidence, declared limitations and release readiness.The current development package is not mainnet-ready. No complete prepared-myosin calculation or validated binding-affinity result is claimed.
05 / FOLLOW THE EVIDENCE
Science you can trace.
The molecular action
of aficamten
Structural and mechanistic investigation of cardiac-myosin inhibition.
NATURE CARDIOVASCULAR RESEARCH · 2024An experimental
structural starting point
Cardiac-myosin coordinates, molecular identity and structural provenance.
RCSB PROTEIN DATA BANK · 9F6CFrom chemical change
to a research question
The published medicinal-chemistry study behind aficamten and its analogues.
JOURNAL OF MEDICINAL CHEMISTRY · 2021$ORVIA / PROPOSED RESEARCH UTILITY
Help decide what
we ask next.
A future research economy built around reviewed experiments, transparent budgets and useful contributions. Explore how $ORVIA could help fund open molecular research.
Explore the $ORVIA proposal Proposed utilities · In development · No funding accepted hereONCHAIN RESEARCH THROUGH VERIFIED INFERENCE AND ANALYSIS
Better questions.
Open possibilities.
Follow the research. Inspect the methods.
Help shape what verifiable molecular science can become.