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Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides.

Publication ,  Journal Article
MacEwan, SR; Weitzhandler, I; Hoffmann, I; Genzer, J; Gradzielski, M; Chilkoti, A
Published in: Biomacromolecules
February 2017

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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Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

February 2017

Volume

18

Issue

2

Start / End Page

599 / 609

Related Subject Headings

  • Transition Temperature
  • Polymers
  • Polymers
  • Phase Transition
  • Peptides
  • Micelles
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • 40 Engineering
  • 34 Chemical sciences
 

Citation

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MacEwan, S. R., Weitzhandler, I., Hoffmann, I., Genzer, J., Gradzielski, M., & Chilkoti, A. (2017). Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides. Biomacromolecules, 18(2), 599–609. https://doi.org/10.1021/acs.biomac.6b01759
MacEwan, Sarah R., Isaac Weitzhandler, Ingo Hoffmann, Jan Genzer, Michael Gradzielski, and Ashutosh Chilkoti. “Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides.Biomacromolecules 18, no. 2 (February 2017): 599–609. https://doi.org/10.1021/acs.biomac.6b01759.
MacEwan SR, Weitzhandler I, Hoffmann I, Genzer J, Gradzielski M, Chilkoti A. Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides. Biomacromolecules. 2017 Feb;18(2):599–609.
MacEwan, Sarah R., et al. “Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides.Biomacromolecules, vol. 18, no. 2, Feb. 2017, pp. 599–609. Epmc, doi:10.1021/acs.biomac.6b01759.
MacEwan SR, Weitzhandler I, Hoffmann I, Genzer J, Gradzielski M, Chilkoti A. Phase Behavior and Self-Assembly of Perfectly Sequence-Defined and Monodisperse Multiblock Copolypeptides. Biomacromolecules. 2017 Feb;18(2):599–609.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

February 2017

Volume

18

Issue

2

Start / End Page

599 / 609

Related Subject Headings

  • Transition Temperature
  • Polymers
  • Polymers
  • Phase Transition
  • Peptides
  • Micelles
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • 40 Engineering
  • 34 Chemical sciences