ArticleBiomacromolecules2017
Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides.
Article in Biomacromolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed.
- The role of the 2'-OH group in phase separation and percolation transitions of RNA.Nature communications · 2026Article
- The Critical Role of the 2'-OH group in Phase Separation and Percolation Transitions of RNA.bioRxiv : the preprint server for biology · 2026Article
- Rational design and preclinical evaluation of elastin-like polypeptide micelle nanoparticles for drug delivery.Frontiers in bioengineering and biotechnology · 2026Review
- Integrating synthetic polypeptides with innovative material forming techniques for advanced biomedical applications.Journal of nanobiotechnology · 2025Review
- Programmability and biomedical utility of intrinsically-disordered protein polymers.Advanced drug delivery reviews · 2024Review
- Adaptive Recombinant Nanoworms from Genetically Encodable Star Amphiphiles.Biomacromolecules · 2022Article
- Refining the Design of Diblock Elastin-Like Polypeptides for Self-Assembly into Nanoparticles.Polymers · 2021Article
- Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021Review
- De novo engineering of intracellular condensates using artificial disordered proteins.Nature chemistry · 2020Article
- Engineering the Architecture of Elastin-Like Polypeptides: From Unimers to Hierarchical Self-Assembly.Advanced therapeutics · 2020Article
- Intrinsically disordered proteins access a range of hysteretic phase separation behaviors.Science advances · 2019Article
- Inducible Fibril Formation of Silk-Elastin Diblocks.ACS omega · 2019Article
- Self-assembly in elastin-like recombinamers: a mechanism to mimic natural complexity.Materials today. Bio · 2019Review
- Active Targeting of Cancer Cells by Nanobody Decorated Polypeptide Micelle with Bio-orthogonally Conjugated Drug.Nano letters · 2019Article
- Author Correction: Injectable tissue integrating networks from recombinant polypeptides with tunable order.Nature materials · 2018Article
- Injectable tissue integrating networks from recombinant polypeptides with tunable order.Nature materials · 2018Article
- Self-assembly/disassembly hysteresis of nanoparticles composed of marginally soluble, short elastin-like polypeptides.Journal of nanobiotechnology · 2018Article
- Article
- Recombinant Synthesis of Hybrid Lipid-Peptide Polymer Fusions that Self-Assemble and Encapsulate Hydrophobic Drugs.Angewandte Chemie (International ed. in English) · 2017Article
- Spontaneous Self-Organized Order Emerging From Intrinsically Disordered Protein Polymers.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
This paper investigates how the properties of multiblock copolypeptides can be tuned by their block architecture, defined by the size and distribution of blocks along the polymer chain. These parameters were explored by the precise, genetically encoded synthesis of recombinant elastin-like polypeptides (ELPs). A family of ELPs was synthesized in which the composition and length were conserved while the block length and distribution were varied, thus creating 11 ELPs with unique block architectures. To our knowledge, these polymers are unprecedented in their intricately and precisely varied architectures. ELPs exhibit lower critical solution temperature (LCST) behavior and micellar self-assembly, both of which impart easily measured physicochemical properties to the copolymers, providing insight into polymer hydrophobicity and self-assembly into higher order structures, as a function of solution temperature. Even subtle variation in block architecture changed the LCST phase behavior and morphology of these ELPs, measured by their temperature-triggered phase transition and nanoscale self-assembly. Size and morphology of polypeptide micelles could be tuned solely by controlling the block architecture, thus demonstrating that when sequence can be precisely controlled, nanoscale self-assembly of polypeptides can be modulated by block architecture.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.