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Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide.

Publication ,  Journal Article
Willems, L; van Westerveld, L; Roberts, S; Weitzhandler, I; Calcines Cruz, C; Hernandez-Garcia, A; Chilkoti, A; Mastrobattista, E; de Vries, R ...
Published in: Biomacromolecules
October 2019

Consensus motifs for sequences of both crystallizable and amorphous blocks in silks and natural structural analogues of silks vary widely. To design novel silklike polypeptides, an important question is therefore how the nature of either the crystallizable or the amorphous block affects the self-assembly and resulting physical properties of silklike polypeptides. We address herein the influence of the amorphous block on the self-assembly of a silklike polypeptide that was previously designed to encapsulate single DNA molecules into rod-shaped viruslike particles. The polypeptide has a triblock architecture, with a long N-terminal amorphous block, a crystallizable midblock, and a C-terminal DNA-binding block. We compare the self-assembly behavior of a triblock with a very hydrophilic collagen-like amorphous block (GXaaYaa)132 to that of a triblock with a less hydrophilic elastin-like amorphous block (GSGVP)80. The amorphous blocks have similar lengths and both adopt a random coil structure in solution. Nevertheless, atomic force microscopy revealed significant differences in the self-assembly behavior of the triblocks. If collagen-like amorphous blocks are used, there is a clear distinction between very short polypeptide-only fibrils and much longer fibrils with encapsulated DNA. If elastin-like amorphous blocks are used, DNA is still encapsulated, but the polypeptide-only fibrils are now much longer and their size distribution partially overlaps with that of the encapsulated DNA fibrils. We attribute the difference to the more hydrophilic nature of the collagen-like amorphous block, which more strongly opposes the growth of polypeptide-only fibrils than the elastin-like amorphous blocks. Our work illustrates that differences in the chemical nature of amorphous blocks can strongly influence the self-assembly and hence the functionality of engineered silklike polypeptides.

Duke Scholars

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

October 2019

Volume

20

Issue

10

Start / End Page

3641 / 3647

Related Subject Headings

  • Silk
  • Protein Multimerization
  • Polymers
  • Peptides
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • DNA, Viral
  • Crystallization
  • Collagen
  • Capsid Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Willems, L., van Westerveld, L., Roberts, S., Weitzhandler, I., Calcines Cruz, C., Hernandez-Garcia, A., … de Vries, R. (2019). Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide. Biomacromolecules, 20(10), 3641–3647. https://doi.org/10.1021/acs.biomac.9b00512
Willems, Lione, Larissa van Westerveld, Stefan Roberts, Isaac Weitzhandler, Carlos Calcines Cruz, Armando Hernandez-Garcia, Ashutosh Chilkoti, Enrico Mastrobattista, John van der Oost, and Renko de Vries. “Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide.Biomacromolecules 20, no. 10 (October 2019): 3641–47. https://doi.org/10.1021/acs.biomac.9b00512.
Willems L, van Westerveld L, Roberts S, Weitzhandler I, Calcines Cruz C, Hernandez-Garcia A, et al. Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide. Biomacromolecules. 2019 Oct;20(10):3641–7.
Willems, Lione, et al. “Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide.Biomacromolecules, vol. 20, no. 10, Oct. 2019, pp. 3641–47. Epmc, doi:10.1021/acs.biomac.9b00512.
Willems L, van Westerveld L, Roberts S, Weitzhandler I, Calcines Cruz C, Hernandez-Garcia A, Chilkoti A, Mastrobattista E, van der Oost J, de Vries R. Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide. Biomacromolecules. 2019 Oct;20(10):3641–3647.
Journal cover image

Published In

Biomacromolecules

DOI

EISSN

1526-4602

ISSN

1525-7797

Publication Date

October 2019

Volume

20

Issue

10

Start / End Page

3641 / 3647

Related Subject Headings

  • Silk
  • Protein Multimerization
  • Polymers
  • Peptides
  • Hydrophobic and Hydrophilic Interactions
  • Elastin
  • DNA, Viral
  • Crystallization
  • Collagen
  • Capsid Proteins