2026-05-18 バージニア工科大学（VirginiaTech）
＜関連情報＞
- https://news.vt.edu/articles/2026/05/science-chemistry-polymers-molecularmatches.html
- https://onlinelibrary.wiley.com/doi/10.1002/anie.202520032
蛍光タンパク質を認識・調節するためのポリアクリレート組成の調整 Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins
Darwin C. Gomez, Swarnadeep Seth, Ronnie Mondal, Stephen J. Koehler, Jared G. Baker, Charles Plate, Ian C. Anderson, Mikayla R. Smith, Joey Gloriod, Morgan Gunter, Valerie V. Welborn
Angewandte Chemie International Edition Published: 17 November 2025
DOI:https://doi.org/10.1002/anie.202520032
Graphical Abstract
Random hetero oligomers (RHOs) of defined compositions are synthesized and fractionated to identify the chemical design criteria (charge, length, hydrophobicity) required to achieve nanomolar binding to green fluorescent protein, resulting in >100% fluorescence increases.
Abstract
Molecular definition is usually regarded as a prerequisite to achieve protein recognition and functional modulation, particularly for macromolecular interactions. Herein, we report that polymers with specific combinations of monomers arranged into random sequences [random hetero oligomers (RHOs)] can selectively bind to a model protein. Using green fluorescent protein (GFP) as a target, polyacrylates were developed that bound with nanomolar affinity and enhanced fluorescence by >100%. Purification of the polymerization product revealed subpopulations of compositions with distinct affinities and selectivity for GFP over a competing protein. Experimental and computational binding analyses confirmed that there are distinct RHO–GFP interactions, which are influenced by RHO chemical composition. These findings show that sequence-defined structures are not a prerequisite for selective protein recognition. Synthetic polymers can instead serve as scalable, tunable platforms for molecular recognition—representing a significant leap towards next-generation sensing, therapeutic, responsive, and catalytic materials in domains previously dominated by biologics or complex peptide scaffolds.
