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Large Language Model is Secretly a Protein Sequence Optimizer (2501.09274v2)

Published 16 Jan 2025 in cs.LG, cs.AI, and q-bio.QM

Abstract: We consider the protein sequence engineering problem, which aims to find protein sequences with high fitness levels, starting from a given wild-type sequence. Directed evolution has been a dominating paradigm in this field which has an iterative process to generate variants and select via experimental feedback. We demonstrate LLMs, despite being trained on massive texts, are secretly protein sequence optimizers. With a directed evolutionary method, LLM can perform protein engineering through Pareto and experiment-budget constrained optimization, demonstrating success on both synthetic and experimental fitness landscapes.

Summary

  • The paper demonstrates that pre-trained LLMs guide protein sequence optimization by outperforming conventional directed evolution on complex fitness landscapes.
  • It introduces an LLM-guided method that diversifies sequences via mutation and crossover, using rejection sampling and Pareto frontier analysis for robust candidate selection.
  • The study implies that integrating LLMs into protein engineering can reduce experimental costs and accelerate the discovery of high-fitness protein variants.

LLM as a Protein Sequence Optimizer

The paper "LLM is Secretly a Protein Sequence Optimizer" demonstrates the application of LLMs in the field of protein engineering—a domain traditionally dominated by directed evolution methodologies. This novel approach addresses the protein sequence engineering challenge by utilizing LLMs trained on extensive text corpora for the optimization of protein sequences, revealing their potential utility as efficient sequence optimizers.

Problem Statement and Background

Protein engineering aims to construct protein sequences that exhibit enhanced functionalities or novel attributes. Directed evolution, a classic method in this discipline, involves iterative rounds of mutagenesis and subsequent selection based on empirical data to generate variants with improved fitness. Despite its success, the greedy nature of directed evolution often results in convergence towards suboptimal fitness peaks within the sequence landscape, which are local maxima rather than global optima. This limitation has prompted interest in integrating machine learning models, such as sequence-to-function predictor models, as surrogates in experimental design processes within directed evolution.

In recent years, advancements like AlphaFold2 have reinvigorated interest in protein LLMs (PLMs) and their capabilities to predict protein structures. Inspired by the successful pre-training strategies for sequence-based tasks, similar techniques have been proposed for protein sequence optimization using pretrained LLMs. Heretofore, its application in protein engineering was conjectural, motivating this research to empirically demonstrate the efficacy of LLMs in such tasks.

Methodology

The authors propose an LLM-guided directed evolutionary method to address single-objective, constrained, budget-constrained, and multi-objective optimization tasks for protein sequence engineering. LLMs are leveraged to generate potential protein sequence variants without additional fine-tuning, relying solely on sampling from the pre-trained models.

  • Initialization: An initial candidate pool is randomly sampled from the sequence space or generated through single mutations of the wild-type protein.
  • Sequence Diversification: LLMs propose new sequences through mutation and crossover mechanisms informed by protein evolutionary principles. The task is framed to allow the LLM to generate novel candidate sequences that demonstrate high fitness and minimal divergence from the reference sequence.
  • Selection Strategy: For single-objective optimization, candidates are ranked based on fitness, employing rejection sampling techniques in constrained optimization to discard non-compliant mutants. Multi-objective scenarios employ Pareto frontier analysis and objective scalarization for selection refinement.

Experiments and Results

The experimental evaluation spans five distinct datasets, employing different oracle functions to model fitness landscapes: exact oracles derived from empirical data, synthetic SLIP model oracles, and machine learning-based oracles. These datasets include landscapes with varying complexities and mutation site allowances, providing a robust assessment of the LLM's performance.

Empirical results indicate that LLM-guided strategy generally surpasses traditional evolutionary algorithms, especially on complex fitness landscapes with larger mutation allowances and nonlinear characteristics. Detailed comparisons reveal that LLMs can effectively navigate these landscapes, yielding variants with superior fitness profiles. In budget-constrained and multi-objective settings, the LLM excels in proposing efficient variant candidates and identifying Pareto-optimal solutions.

Implications and Future Work

This paper highlights the potential of LLMs as powerful tools for optimizing protein sequences, encouraging a shift towards integrating text-trained LLMs into biotechnological applications. This alignment with protein structure and functional optimization could pave the way for more computationally efficient experimental designs, reducing dependency on exhaustive laboratory validation.

The research opens several avenues for future exploration, including the integration of LLMs with real-time experimental feedback and adaptive learning strategies, enhancing both exploration efficiency and sequence diversity. Extending LLM applications in protein engineering, alongside advancements in model architecture and training regimes, could significantly influence future directions in artificial intelligence's application in biological sciences.