Monomer‐scale design of functional protein polymers using consensus repeat sequences

Chang, Marina P.; Huang, Winnie; Mai, Danielle J.

doi:10.1002/pol.20210506

Cited by 20Advanced Polymer Synthesis and CharacterizationPolymer Surface Interaction StudiesSilk-based biomaterials and applications

Monomer‐scale design of functional protein polymers using consensus repeat sequences

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Chang, Marina P., Huang, Winnie, Mai, Danielle J.·2021·Journal of Polymer Science

DOI 10.1002/pol.20210506

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Abstract

Protein‐based polymers possess chemically defined sequences that can encode diverse properties and functions into a new class of biopolymeric materials. However, sequence variation that emerges from evolution can obscure the sequence–function relationships of naturally derived polymers. One strategy to clarify these relationships is to identify common sequences between proteins with similar functions. These conserved sequences often emerge from repeat proteins, and “consensus repeat sequences” provide a convenient platform for systematic investigations of biopolymer sequence–property relationships. In this review, we highlight recent approaches to engineer tunable polymeric materials using monomer‐scale design of consensus repeat proteins. We explore established and emerging protein‐based materials with mechanical resilience, thermodynamic phase behavior, chemical responsiveness, biomolecular transport, and hierarchical structure. Overall, recent advances in the monomer‐scale design of repetitive protein polymers present exciting fundamental and translational opportunities for polymer scientists and engineers.

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Consensus sequences determined by multiple sequence alignment are believed to play a crucial part in maintaining protein stability and adhesion throughout evolution.
“We then performed multiple sequence alignment using Clustal Omega23 to determine consensus sequences for each species (Extended Data Fig. 1), which are believed to play a crucial part in maintaining protein stability and adhesion throughout evolution24,25.”
From Data-driven de novo design of super-adhesive hydrogels (2025) · cites this paper as [25]
The Introduction says that alignment identifies conserved amino acids that help preserve protein stability and function during evolution. It does not specifically say that consensus sequences maintain adhesion throughout evolution; the adhesion claim is unsupported by the passages located in our copy. (LLM, conf=0.85)
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Authors: Chang, M. P., Huang, W., & Mai, D. J.
Affiliations: Stanford University (US)
Corresponding author: Mai, Danielle J.
ORCID: Chang, Marina P.
Huang, Winnie
Mai, Danielle J.
Venue: Journal of Polymer Science
Publisher: Wiley
Published: 2021-09-30
Volume: 59
Issue: 22
Pages: 2644-2664
ISSN: 2642-4150 (ISSN-L)
2642-4169
DOI: 10.1002/pol.20210506
OpenAlex: W3203656172
Cited by: 20
References: 260
Citations by year: 2026: 3 · 2025: 6 · 2024: 5 · 2023: 1 · 2022: 5
FWCI: 1.09
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#am (am, 365 d)
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Journal of Polymer Science (publishedVersion)
OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders: Basic Energy Sciences (DE‐AC02‐76SF00515)
Topics: Physical Sciences › Chemistry › Organic Chemistry › Advanced Polymer Synthesis and Characterization
Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords: protein polymers, sequence-function relationships, repeat proteins, protein self-assembly, mechanical resilience, biomolecular transport, hierarchy, biopolymers

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Monomer‐scale design of functional protein polymers using consensus repeat sequences

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