Self-assembly of temperature-responsive protein-polymer bioconjugates

Research output: Contribution to journalArticlepeer-review

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Self-assembly of temperature-responsive protein-polymer bioconjugates. / Moatsou, Dafni; Li, Jian; Ranji, Arnaz; Pitto-Barry, Anais; Ntai, Ioanna; Jewett, Michael C.; O'Reilly, Rachel K.

In: Bioconjugate Chemistry, Vol. 26, No. 9, 16.09.2015, p. 1890-1899.

Research output: Contribution to journalArticlepeer-review

Harvard

Moatsou, D, Li, J, Ranji, A, Pitto-Barry, A, Ntai, I, Jewett, MC & O'Reilly, RK 2015, 'Self-assembly of temperature-responsive protein-polymer bioconjugates', Bioconjugate Chemistry, vol. 26, no. 9, pp. 1890-1899. https://doi.org/10.1021/acs.bioconjchem.5b00264

APA

Vancouver

Moatsou D, Li J, Ranji A, Pitto-Barry A, Ntai I, Jewett MC et al. Self-assembly of temperature-responsive protein-polymer bioconjugates. Bioconjugate Chemistry. 2015 Sep 16;26(9):1890-1899. https://doi.org/10.1021/acs.bioconjchem.5b00264

Author

Moatsou, Dafni ; Li, Jian ; Ranji, Arnaz ; Pitto-Barry, Anais ; Ntai, Ioanna ; Jewett, Michael C. ; O'Reilly, Rachel K. / Self-assembly of temperature-responsive protein-polymer bioconjugates. In: Bioconjugate Chemistry. 2015 ; Vol. 26, No. 9. pp. 1890-1899.

Bibtex

@article{8c09e4f73dfa4d4ba0bc08f36daec4df,
title = "Self-assembly of temperature-responsive protein-polymer bioconjugates",
abstract = "We report a simple temperature-responsive bioconjugate system comprising superfolder green fluorescent protein (sfGFP) decorated with poly[(oligo ethylene glycol) methyl ether methacrylate] (PEGMA) polymers. We used amber suppression to site-specifically incorporate the non-canonical azide-functional amino acid p-azidophenylalanine (pAzF) into sfGFP at different positions. The azide moiety on modified sfGFP was then coupled using copper-catalyzed “click” chemistry with the alkyne terminus of a PEGMA synthesized by reversible addition–fragmentation chain transfer (RAFT) polymerization. The protein in the resulting bioconjugate was found to remain functionally active (i.e., fluorescent) after conjugation. Turbidity measurements revealed that the point of attachment of the polymer onto the protein scaffold has an impact on the thermoresponsive behavior of the resultant bioconjugate. Furthermore, small-angle X-ray scattering analysis showed the wrapping of the polymer around the protein in a temperature-dependent fashion. Our work demonstrates that standard genetic manipulation combined with an expanded genetic code provides an easy way to construct functional hybrid biomaterials where the location of the conjugation site on the protein plays an important role in determining material properties. We anticipate that our approach could be generalized for the synthesis of complex functional materials with precisely defined domain orientation, connectivity, and composition.",
author = "Dafni Moatsou and Jian Li and Arnaz Ranji and Anais Pitto-Barry and Ioanna Ntai and Jewett, {Michael C.} and O'Reilly, {Rachel K.}",
year = "2015",
month = sep,
day = "16",
doi = "10.1021/acs.bioconjchem.5b00264",
language = "English",
volume = "26",
pages = "1890--1899",
journal = "Bioconjugate Chemistry",
issn = "1043-1802",
publisher = "American Chemical Society",
number = "9",

}

RIS

TY - JOUR

T1 - Self-assembly of temperature-responsive protein-polymer bioconjugates

AU - Moatsou, Dafni

AU - Li, Jian

AU - Ranji, Arnaz

AU - Pitto-Barry, Anais

AU - Ntai, Ioanna

AU - Jewett, Michael C.

AU - O'Reilly, Rachel K.

PY - 2015/9/16

Y1 - 2015/9/16

N2 - We report a simple temperature-responsive bioconjugate system comprising superfolder green fluorescent protein (sfGFP) decorated with poly[(oligo ethylene glycol) methyl ether methacrylate] (PEGMA) polymers. We used amber suppression to site-specifically incorporate the non-canonical azide-functional amino acid p-azidophenylalanine (pAzF) into sfGFP at different positions. The azide moiety on modified sfGFP was then coupled using copper-catalyzed “click” chemistry with the alkyne terminus of a PEGMA synthesized by reversible addition–fragmentation chain transfer (RAFT) polymerization. The protein in the resulting bioconjugate was found to remain functionally active (i.e., fluorescent) after conjugation. Turbidity measurements revealed that the point of attachment of the polymer onto the protein scaffold has an impact on the thermoresponsive behavior of the resultant bioconjugate. Furthermore, small-angle X-ray scattering analysis showed the wrapping of the polymer around the protein in a temperature-dependent fashion. Our work demonstrates that standard genetic manipulation combined with an expanded genetic code provides an easy way to construct functional hybrid biomaterials where the location of the conjugation site on the protein plays an important role in determining material properties. We anticipate that our approach could be generalized for the synthesis of complex functional materials with precisely defined domain orientation, connectivity, and composition.

AB - We report a simple temperature-responsive bioconjugate system comprising superfolder green fluorescent protein (sfGFP) decorated with poly[(oligo ethylene glycol) methyl ether methacrylate] (PEGMA) polymers. We used amber suppression to site-specifically incorporate the non-canonical azide-functional amino acid p-azidophenylalanine (pAzF) into sfGFP at different positions. The azide moiety on modified sfGFP was then coupled using copper-catalyzed “click” chemistry with the alkyne terminus of a PEGMA synthesized by reversible addition–fragmentation chain transfer (RAFT) polymerization. The protein in the resulting bioconjugate was found to remain functionally active (i.e., fluorescent) after conjugation. Turbidity measurements revealed that the point of attachment of the polymer onto the protein scaffold has an impact on the thermoresponsive behavior of the resultant bioconjugate. Furthermore, small-angle X-ray scattering analysis showed the wrapping of the polymer around the protein in a temperature-dependent fashion. Our work demonstrates that standard genetic manipulation combined with an expanded genetic code provides an easy way to construct functional hybrid biomaterials where the location of the conjugation site on the protein plays an important role in determining material properties. We anticipate that our approach could be generalized for the synthesis of complex functional materials with precisely defined domain orientation, connectivity, and composition.

UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:000361503100006&KeyUID=WOS:000361503100006

U2 - 10.1021/acs.bioconjchem.5b00264

DO - 10.1021/acs.bioconjchem.5b00264

M3 - Article

VL - 26

SP - 1890

EP - 1899

JO - Bioconjugate Chemistry

JF - Bioconjugate Chemistry

SN - 1043-1802

IS - 9

ER -