Literature DB >> 29895685

Efficient encapsulation of proteins with random copolymers.

Trung Dac Nguyen1, Baofu Qiao1, Monica Olvera de la Cruz2,3,4.   

Abstract

Membraneless organelles are aggregates of disordered proteins that form spontaneously to promote specific cellular functions in vivo. The possibility of synthesizing membraneless organelles out of cells will therefore enable fabrication of protein-based materials with functions inherent to biological matter. Since random copolymers contain various compositions and sequences of solvophobic and solvophilic groups, they are expected to function in nonbiological media similarly to a set of disordered proteins in membraneless organelles. Interestingly, the internal environment of these organelles has been noted to behave more like an organic solvent than like water. Therefore, an adsorbed layer of random copolymers that mimics the function of disordered proteins could, in principle, protect and enhance the proteins' enzymatic activity even in organic solvents, which are ideal when the products and/or the reactants have limited solubility in aqueous media. Here, we demonstrate via multiscale simulations that random copolymers efficiently incorporate proteins into different solvents with the potential to optimize their enzymatic activity. We investigate the key factors that govern the ability of random copolymers to encapsulate proteins, including the adsorption energy, copolymer average composition, and solvent selectivity. The adsorbed polymer chains have remarkably similar sequences, indicating that the proteins are able to select certain sequences that best reduce their exposure to the solvent. We also find that the protein surface coverage decreases when the fluctuation in the average distance between the protein adsorption sites increases. The results herein set the stage for computational design of random copolymers for stabilizing and delivering proteins across multiple media.

Entities:  

Keywords:  coarse-grained molecular simulations; protein stabilization; protein surface pattern; random copolymers

Mesh:

Substances:

Year:  2018        PMID: 29895685      PMCID: PMC6042061          DOI: 10.1073/pnas.1806207115

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  20 in total

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5.  Random copolymers that protect proteins.

Authors:  Alfredo Alexander-Katz; Reid C Van Lehn
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6.  Random heteropolymers preserve protein function in foreign environments.

Authors:  Brian Panganiban; Baofu Qiao; Tao Jiang; Christopher DelRe; Mona M Obadia; Trung Dac Nguyen; Anton A A Smith; Aaron Hall; Izaac Sit; Marquise G Crosby; Patrick B Dennis; Eric Drockenmuller; Monica Olvera de la Cruz; Ting Xu
Journal:  Science       Date:  2018-03-16       Impact factor: 47.728

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Review 8.  Protein misfolding and aggregation in cataract disease and prospects for prevention.

Authors:  Kate L Moreau; Jonathan A King
Journal:  Trends Mol Med       Date:  2012-04-19       Impact factor: 11.951

9.  Strong Selective Adsorption of Polymers.

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Journal:  Macromolecules       Date:  2015-05-20       Impact factor: 5.985

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Authors:  Timothy J Nott; Evangelia Petsalaki; Patrick Farber; Dylan Jervis; Eden Fussner; Anne Plochowietz; Timothy D Craggs; David P Bazett-Jones; Tony Pawson; Julie D Forman-Kay; Andrew J Baldwin
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4.  Functional enzyme-polymer complexes.

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