Random heteropolymers preserve protein function in foreign environments
Abstract
Mimicking the designs found in proteins: Natural proteins combine a range of useful features, including chemical diversity, the ability to rapidly switch between preprogrammed shapes, and a hierarchy of structures. Panganiban et al. designed random copolymers with polar and nonpolar groups, using many of the features found in proteins (see the Perspective by Alexander-Katz and Van Lehn). Their structures could serve as “broad spectrum” surfactants, able to promote the solubilization of proteins in organic solvents and help preserve the functionality of proteins in aqueous environments. Science , this issue p. 1239 ; see also p. 1216
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Ideal random copolymerization of the six functional monomers has minimal composition drift during polymerization and enables statistically controlled sequences.
“Therefore, we aimed to statistically replicate the sequence features of functional classes through ideal random copolymerization of the six functional monomers, which has minimal composition drift during polymerization and enables statistically controlled sequences19,27–29.”
From Data-driven de novo design of super-adhesive hydrogels (2025) · cites this paper as [28]
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- Authors
- Panganiban, B., Qiao, B., Jiang, T., DelRe, C., Obadia, M. M., Nguyen, T. D., Smith, A. A. A., Hall, A., Sit, I., Crosby, M. G., Dennis, P. B., Drockenmuller, E., Olvera de la Cruz, M., & Xu, T.
- Affiliations
- University of California, Berkeley (US)
- Northwestern University (US)
- Lyon 1 Université (FR)
- Department of Materials Science and Engineering, University of California, Berkeley, Berkeley, CA 94720, USA.
- United States Air Force Research Laboratory (US)
- Université Lyon, Université Lyon 1, CNRS, Ingénierie des Matériaux Polymères, UMR 5223, F-69003 Lyon, France.
- Department of Materials Science and Engineering, Northwestern University, Evanston, IL 60208, USA.
- Lawrence Berkeley National Laboratory (US)
- Corresponding author
- Xu, Ting
- ORCID
- Venue
- Science
- Published
- 2018-03-16
- Volume
- 359
- Issue
- 6381
- Pages
- 1239-1243
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2794179757
- Cited by
- 294
- References
- 49
- Citations by year
- 2026: 33 · 2025: 40 · 2024: 35 · 2023: 35 · 2022: 44 · 2021: 33 · 2020: 31 · 2019: 27 · 2018: 16
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Sherman Fairchild Foundation
- Department of Defense, Army Research Office (W911NF-13-1-0232)
- Department of Energy Basica Energy Science (DE-FG02-08ER46539)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Physical Sciences › Chemistry › Organic Chemistry › Advanced Polymer Synthesis and Characterization
- Keywords
- random heteropolymers, protein stabilization, intrinsically disordered proteins, protein solubilization, protein folding, cell-free protein synthesis, membrane proteins, protein-based biomaterials
- MeSH terms
- Amino Acid Sequence, Polymers, Proteins, Solubility, Protein Folding, Biomimetic Materials, Molecular Dynamics Simulation
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