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OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
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Mapping protein-polymer conformations in bioconjugates with atomic precision.

Kevin M Burridge1, Ben A Shurina1, Caleb T Kozuszek1

  • 1Department of Chemistry and Biochemistry , Miami University , 651 E High St. , Oxford , OH 45056 , USA . Email: d.konkolewicz@MiamiOH.edu ;

Chemical Science
|September 21, 2020
PubMed
Summary
This summary is machine-generated.

Protein-polymer bioconjugate design is improved using nuclear magnetic resonance (NMR) paramagnetic relaxation enhancement (PRE) to reveal polymer conformation. This interaction stabilizes proteins against denaturation, advancing bioconjugate understanding.

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Area of Science:

  • Bioconjugation Chemistry
  • Polymer Science
  • Structural Biology

Background:

  • Rational design of protein-polymer bioconjugates requires understanding protein-polymer interactions.
  • Limited experimental data and mechanistic insights hinder rational design.

Purpose of the Study:

  • To investigate the conformation of conjugated polymers on proteins using NMR.
  • To elucidate the role of protein-polymer interactions in bioconjugate stability.

Main Methods:

  • Utilized nuclear magnetic resonance (NMR) paramagnetic relaxation enhancement (PRE) to probe distances between spin labels and nuclei.
  • Collected 1H/15N-heteronuclear single quantum coherence (HSQC) NMR spectra for ubiquitin (Ub) modified with block copolymers.
  • Assessed bioconjugate stability against denaturation using circular dichroism (CD).

Main Results:

  • PRE data revealed that conjugated polymers adopt conformations biased towards the nonpolar β-sheet face of ubiquitin.
  • The polymers did not behave as if in solution when attached to the protein.
  • Bioconjugates exhibited enhanced stability against guanidine-hydrochloride-induced denaturation.

Conclusions:

  • Protein-polymer interactions significantly influence conjugated polymer conformation.
  • The observed stabilization of bioconjugates is attributed to these specific interactions.
  • This study provides mechanistic insights for the rational design of protein-polymer bioconjugates.