Skip to main content
construction release_alert
Scholars@Duke will be undergoing maintenance April 11-15. Some features may be unavailable during this time.
cancel
Journal cover image

Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core

Publication ,  Journal Article
Garanger, E; MacEwan, SR; Sandre, O; Brûlet, A; Bataille, L; Chilkoti, A; Lecommandoux, S
Published in: Macromolecules
September 22, 2015

With a perfectly defined primary structure, both in terms of monomer sequence and chain length, recombinant polypeptides obtained by protein engineering techniques allow the investigation of structure-property relationships at a level of detail that is difficult to achieve with traditional synthetic polymers because of the precision with which their sequence can be defined. In the present work, we have studied the behavior and temperature-triggered self-assembly of a series of diblock recombinant elastin-like polypeptides (ELPs) with the goal of elucidating the mechanism of their self-assembly into micelles. Aqueous solutions of diblock ELPs were studied below and above their critical micellar temperature (CMT) by multiangle light scattering and small-angle neutron scattering techniques. Below the CMT, the radius of gyration of soluble ELP chains follows a power law as a function of molecular weight with an exponent value close to 0.5 that is characteristic of Gaussian coil conformations. As the temperature reaches the CMT, attractive interactions between the more hydrophobic block of diblock ELP chains leads to the self-assembly of monodisperse spherical micelles at thermodynamic equilibrium. Above the CMT, micelles expel water molecules from their core whose densification is evidenced by the monotonic increase in the light and neutron scattering intensities as a function of temperature. The behaviors of these different diblock ELPs in solution and as self-assembled nanoparticles above the CMT following universal experimental scaling laws make them analogous to synthetic amphiphilic diblock copolymers (star-like vs crew-cut micelle models). These studies also shed light on the important role of water in the thermal behavior of these thermally responsive self-assembling diblock polypeptides and suggest a new design parameter-thermally triggered desolvation and densification of the core of micelles-that can be fine-tuned at the sequence level to control the density of self-assembled polymer nanoparticles.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Macromolecules

DOI

EISSN

1520-5835

ISSN

0024-9297

Publication Date

September 22, 2015

Volume

48

Issue

18

Start / End Page

6617 / 6627

Related Subject Headings

  • Polymers
  • 40 Engineering
  • 34 Chemical sciences
  • 09 Engineering
  • 03 Chemical Sciences
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Garanger, E., MacEwan, S. R., Sandre, O., Brûlet, A., Bataille, L., Chilkoti, A., & Lecommandoux, S. (2015). Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core. Macromolecules, 48(18), 6617–6627. https://doi.org/10.1021/acs.macromol.5b01371
Garanger, E., S. R. MacEwan, O. Sandre, A. Brûlet, L. Bataille, A. Chilkoti, and S. Lecommandoux. “Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core.” Macromolecules 48, no. 18 (September 22, 2015): 6617–27. https://doi.org/10.1021/acs.macromol.5b01371.
Garanger E, MacEwan SR, Sandre O, Brûlet A, Bataille L, Chilkoti A, et al. Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core. Macromolecules. 2015 Sep 22;48(18):6617–27.
Garanger, E., et al. “Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core.” Macromolecules, vol. 48, no. 18, Sept. 2015, pp. 6617–27. Scopus, doi:10.1021/acs.macromol.5b01371.
Garanger E, MacEwan SR, Sandre O, Brûlet A, Bataille L, Chilkoti A, Lecommandoux S. Structural Evolution of a Stimulus-Responsive Diblock Polypeptide Micelle by Temperature Tunable Compaction of its Core. Macromolecules. 2015 Sep 22;48(18):6617–6627.
Journal cover image

Published In

Macromolecules

DOI

EISSN

1520-5835

ISSN

0024-9297

Publication Date

September 22, 2015

Volume

48

Issue

18

Start / End Page

6617 / 6627

Related Subject Headings

  • Polymers
  • 40 Engineering
  • 34 Chemical sciences
  • 09 Engineering
  • 03 Chemical Sciences