Pareto-Optimal Offline Reinforcement Learning via Smooth Tchebysheff Scalarization

Fuente: arXiv
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Main Authors: Bhatnagar, Aadyot, Groth, Peter Mørch, Madani, Ali
Format: Preprint
Published: 2026
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author Bhatnagar, Aadyot
Groth, Peter Mørch
Madani, Ali
author_facet Bhatnagar, Aadyot
Groth, Peter Mørch
Madani, Ali
contents Large language models can be aligned with human preferences through offline reinforcement learning (RL) on small labeled datasets. While single-objective alignment is well-studied, many real-world applications demand the simultaneous optimization of multiple conflicting rewards, e.g. optimizing both catalytic activity and specificity in protein engineering, or helpfulness and harmlessness for chatbots. Prior work has largely relied on linear reward scalarization, but this approach provably fails to recover non-convex regions of the Pareto front. In this paper, instead of scalarizing the rewards directly, we frame multi-objective RL itself as an optimization problem to be scalarized via smooth Tchebysheff scalarization, a recent technique that overcomes the shortcomings of linear scalarization. We use this formulation to derive Smooth Tchebysheff Optimization of Multi-Objective Preferences (STOMP), a novel offline RL algorithm that extends direct preference optimization to the multi-objective setting in a principled way by standardizing the individual rewards based on their observed distributions. We empirically validate STOMP on a range of protein engineering tasks by aligning three autoregressive protein language models on three laboratory datasets of protein fitness. Compared to state-of-the-art baselines, STOMP achieves the highest hypervolumes in eight of nine settings according to both offline off-policy and generative evaluations. We thus demonstrate that STOMP is a powerful, robust multi-objective alignment algorithm that can meaningfully improve post-trained models for multi-attribute protein optimization and beyond.
format Preprint
id arxiv_https___arxiv_org_abs_2604_13175
institution arXiv
publishDate 2026
record_format arxiv
spellingShingle Pareto-Optimal Offline Reinforcement Learning via Smooth Tchebysheff Scalarization
Bhatnagar, Aadyot
Groth, Peter Mørch
Madani, Ali
Machine Learning
Artificial Intelligence
Biomolecules
Quantitative Methods
Large language models can be aligned with human preferences through offline reinforcement learning (RL) on small labeled datasets. While single-objective alignment is well-studied, many real-world applications demand the simultaneous optimization of multiple conflicting rewards, e.g. optimizing both catalytic activity and specificity in protein engineering, or helpfulness and harmlessness for chatbots. Prior work has largely relied on linear reward scalarization, but this approach provably fails to recover non-convex regions of the Pareto front. In this paper, instead of scalarizing the rewards directly, we frame multi-objective RL itself as an optimization problem to be scalarized via smooth Tchebysheff scalarization, a recent technique that overcomes the shortcomings of linear scalarization. We use this formulation to derive Smooth Tchebysheff Optimization of Multi-Objective Preferences (STOMP), a novel offline RL algorithm that extends direct preference optimization to the multi-objective setting in a principled way by standardizing the individual rewards based on their observed distributions. We empirically validate STOMP on a range of protein engineering tasks by aligning three autoregressive protein language models on three laboratory datasets of protein fitness. Compared to state-of-the-art baselines, STOMP achieves the highest hypervolumes in eight of nine settings according to both offline off-policy and generative evaluations. We thus demonstrate that STOMP is a powerful, robust multi-objective alignment algorithm that can meaningfully improve post-trained models for multi-attribute protein optimization and beyond.
title Pareto-Optimal Offline Reinforcement Learning via Smooth Tchebysheff Scalarization
topic Machine Learning
Artificial Intelligence
Biomolecules
Quantitative Methods
url https://arxiv.org/abs/2604.13175