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Membrane-active Polymers: NCMNP13-x, NCMNP21-x and NCMNP21b-x for Membrane Protein Structural Biology

View ORCID ProfileThi Kim Hoang Trinh, View ORCID ProfileClaudio Catalano, View ORCID ProfileYouzhong Guo
doi: https://doi.org/10.1101/2022.01.10.475744
Thi Kim Hoang Trinh
aDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, USA
bInstitute for Structural Biology, Drug Discovery and Development, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23219, USA
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Claudio Catalano
aDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, USA
bInstitute for Structural Biology, Drug Discovery and Development, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23219, USA
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Youzhong Guo
aDepartment of Medicinal Chemistry, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23298, USA
bInstitute for Structural Biology, Drug Discovery and Development, School of Pharmacy, Virginia Commonwealth University, Richmond, VA 23219, USA
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  • For correspondence: yguo4@vcu.edu
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Abstract

Membrane proteins are a ubiquitous group of bio-macromolecules responsible for many crucial biological processes and serve as drug targets for a wide range of modern drugs. Detergent-free technologies such as styrene-maleic acid lipid particles (SMALP), diisobutylene-maleic acid lipid particles (DIBMALP), and native cell membrane nanoparticles (NCMN) systems have recently emerged as revolutionary alternatives to the traditional detergent-based approaches for membrane protein research. NCMN systems aim to create a membrane-active polymer library suitable for high-resolution structure determination. Herein, we report our design, synthesis, characterization and comparative application analyses of three novel classes of NCMN polymers, NCMNP13-x, NCMNP21-x and NCMNP21b-x. Although each NCMN polymer can solubilize various model membrane proteins and conserve native lipids into NCMN particles, only the NCMNP21b-x series reveals lipid-protein particles with good buffer compatibility and high homogeneity suitable for single-particle cryo-EM analysis. Consequently, the NCMNP21b-x polymers that bring out high-quality NCMN particles are particularly attractive for membrane protein structural biology.

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Highlights

  • Demonstrate straightforward strategies for tailoring styrene-maleic co-polymer (SMA) that revealed novel buffer compatible polymers, NCMNP13-50, NCMNP21-20 and NCMNP21b-x.

  • Elucidate how modification factors alter the membrane-active properties of these polymers, i.e., membrane protein extraction efficiency, morphology, etc.

  • Provide valuable insights into the rational design of membrane-active polymers for membrane protein structural biology.

  • NCMNP21b-x polymers are highly compatible with high-resolution structure determination using an emerging technique, cryo-EM.

Competing Interest Statement

Y.G. and T.K.H.T are inventors of NCMNP13-50, NCMNP21-20 and NCMNP21b-x patents

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted January 11, 2022.
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Membrane-active Polymers: NCMNP13-x, NCMNP21-x and NCMNP21b-x for Membrane Protein Structural Biology
Thi Kim Hoang Trinh, Claudio Catalano, Youzhong Guo
bioRxiv 2022.01.10.475744; doi: https://doi.org/10.1101/2022.01.10.475744
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Membrane-active Polymers: NCMNP13-x, NCMNP21-x and NCMNP21b-x for Membrane Protein Structural Biology
Thi Kim Hoang Trinh, Claudio Catalano, Youzhong Guo
bioRxiv 2022.01.10.475744; doi: https://doi.org/10.1101/2022.01.10.475744

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