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Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides.

Publication ,  Journal Article
Li, NK; Roberts, S; Quiroz, FG; Chilkoti, A; Yingling, YG
Published in: Biomacromolecules
July 2018

Elastin-like polypeptides (ELP) exhibit an inverse temperature transition or lower critical solution temperature (LCST) transition phase behavior in aqueous solutions. In this paper, the thermal responsive properties of the canonical ELP, poly(VPGVG), and its reverse sequence poly(VGPVG) were investigated by turbidity measurements of the cloud point behavior, circular dichroism (CD) measurements, and all-atom molecular dynamics (MD) simulations to gain a molecular understanding of mechanism that controls hysteretic phase behavior. It was shown experimentally that both poly(VPGVG) and poly(VGPVG) undergo a transition from soluble to insoluble in aqueous solution upon heating above the transition temperature ( Tt). However, poly(VPGVG) resolubilizes upon cooling below its Tt, whereas the reverse sequence, poly(VGPVG), remains aggregated despite significant undercooling below the Tt. The results from MD simulations indicated that a change in sequence order results in significant differences in the dynamics of the specific residues, especially valines, which lead to extensive changes in the conformations of VPGVG and VGPVG pentamers and, consequently, dissimilar propensities for secondary structure formation and overall structure of polypeptides. These changes affected the relative hydrophilicities of polypeptides above Tt, where poly(VGPVG) is more hydrophilic than poly(VPGVG) with more extended conformation and larger surface area, which led to formation of strong interchain hydrogen bonds responsible for stabilization of the aggregated phase and the observed thermal hysteresis for poly(VGPVG).

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Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

July 2018

Volume

19

Issue

7

Start / End Page

2496 / 2505

Related Subject Headings

  • Temperature
  • Protein Domains
  • Polymers
  • Phase Transition
  • Molecular Dynamics Simulation
  • Elastin
  • Amino Acid Motifs
  • 40 Engineering
  • 34 Chemical sciences
  • 31 Biological sciences
 

Citation

APA
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ICMJE
MLA
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Li, N. K., Roberts, S., Quiroz, F. G., Chilkoti, A., & Yingling, Y. G. (2018). Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides. Biomacromolecules, 19(7), 2496–2505. https://doi.org/10.1021/acs.biomac.8b00099
Li, Nan K., Stefan Roberts, Felipe Garcia Quiroz, Ashutosh Chilkoti, and Yaroslava G. Yingling. “Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides.Biomacromolecules 19, no. 7 (July 2018): 2496–2505. https://doi.org/10.1021/acs.biomac.8b00099.
Li NK, Roberts S, Quiroz FG, Chilkoti A, Yingling YG. Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides. Biomacromolecules. 2018 Jul;19(7):2496–505.
Li, Nan K., et al. “Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides.Biomacromolecules, vol. 19, no. 7, July 2018, pp. 2496–505. Epmc, doi:10.1021/acs.biomac.8b00099.
Li NK, Roberts S, Quiroz FG, Chilkoti A, Yingling YG. Sequence Directionality Dramatically Affects LCST Behavior of Elastin-Like Polypeptides. Biomacromolecules. 2018 Jul;19(7):2496–2505.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

July 2018

Volume

19

Issue

7

Start / End Page

2496 / 2505

Related Subject Headings

  • Temperature
  • Protein Domains
  • Polymers
  • Phase Transition
  • Molecular Dynamics Simulation
  • Elastin
  • Amino Acid Motifs
  • 40 Engineering
  • 34 Chemical sciences
  • 31 Biological sciences