Random heteropolymers as enzyme mimics
Random heteropolymers as enzyme mimics
Breslow, R. Artificial enzymes. Science 218, 532–537 (1982).
DeGrado, W. F., Wasserman, Z. R. & Lear, J. D. Protein design, a minimalist approach. Science 243, 622–628 (1989).
Kuhlman, B. et al. Design of a novel globular protein fold with atomic-level accuracy. Science 302, 1364–1368 (2003).
Castriciano, M. A., Romeo, A., Baratto, M. C., Pogni, R. & Scolaro, L. M. Supramolecular mimetic peroxidase based on hemin and PAMAM dendrimers. Chem. Commun. 14, 688–690 (2008).
Schmidt, B. V. K. J., Fechler, N., Falkenhagen, J. & Lutz, J.-F. Controlled folding of synthetic polymer chains through the formation of positionable covalent bridges. Nat. Chem. 3, 234–238 (2011).
Terashima, T. et al. Single-chain folding of polymers for catalytic systems in water. J. Am. Chem. Soc. 133, 4742–4745 (2011).
Wiester, M. J., Ulmann, P. A. & Mirkin, C. A. Enzyme mimics based upon supramolecular coordination chemistry. Angew. Chem. Int. Ed. 50, 114–137 (2011).
Kaphan, D. M., Levin, M. D., Bergman, R. G., Raymond, K. N. & Toste, F. D. A supramolecular microenvironment strategy for transition metal catalysis. Science 350, 1235–1238 (2015).
Nath, I., Chakraborty, J. & Verpoort, F. Metal organic frameworks mimicking natural enzymes: a structural and functional analogy. Chem. Soc. Rev. 45, 4127–4170 (2016).
Liu, Q., Wang, H., Shi, X. H., Wang, Z.-G. & Ding, B. Q. Self-assembled DNA/peptide-based nanoparticle exhibiting synergistic enzymatic activity. ACS Nano 11, 7251–7258 (2017).
Mundsinger, K., Izuagbe, A., Tuten, B. T., Roesky, P. W. & Barner-Kowollik, C. Single chain nanoparticles in catalysis. Angew. Chem. Int. Ed. 63, e202311734 (2024).
Lutz, J.-F., Ouchi, M., Liu, D. R. & Sawamoto, M. Sequence-controlled polymers. Science 341, 1238149 (2013).
Lombardi, A., Pirro, F., Maglio, O., Chino, M. & DeGrado, W. F. De novo design of four-helix bundle metalloproteins: one scaffold, diverse reactivities. Acc. Chem. Res. 52, 1148–1159 (2019).
Rose, G. D., Fleming, P. J., Banavar, J. R. & Maritan, A. A backbone-based theory of protein folding. Proc. Natl Acad. Sci. USA 103, 16623–16633 (2006).
Zaccai, G. How soft is a protein? A protein dynamics force constant measured by neutron scattering. Science 288, 1604–1607 (2000).
Henzler-Wildman, K. & Kern, D. Dynamic personalities of proteins. Nature 450, 964–972 (2007).
Magazù, S. et al. Protein dynamics as seen by (quasi) elastic neutron scattering. Biochim. Biophys. Acta Gen. Subj. 1861, 3504–3512 (2017).
Robertson, D. E. et al. Design and synthesis of multi-haem proteins. Nature 368, 425–432 (1994).
Sugase, K., Dyson, H. J. & Wright, P. E. Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447, 1021–1025 (2007).
Hilburg, S. L., Ruan, Z., Xu, T. & Alexander-Katz, A. Behavior of protein-inspired synthetic random heteropolymers. Macromolecules 53, 9187–9199 (2020).
Jiang, T. et al. Single-chain heteropolymers transport protons selectively and rapidly. Nature 577, 216–220 (2020).
Daghrir, R. & Drogui, P. Tetracycline antibiotics in the environment: a review. Environ. Chem. Lett. 11, 209–227 (2013).
Dill, K. A. et al. Principles of protein folding — a perspective from simple exact models. Protein Sci. 4, 561–602 (1995).
Ruan, Z. et al. Population-based heteropolymer design to mimic protein mixtures. Nature 615, 251–258 (2023).
Artar, M., Souren, E. R. J., Terashima, T., Meijer, E. W. & Palmans, A. R. A. Single chain polymeric nanoparticles as selective hydrophobic reaction spaces in water. ACS Macro Lett. 4, 1099–1103 (2015).
Hoshino, Y. et al. The rational design of a synthetic polymer nanoparticle that neutralizes a toxic peptide in vivo. Proc. Natl Acad. Sci. USA 109, 33–38 (2012).
Popot, J.-L. et al. Amphipols from A to Z. Annu. Rev. Biophys. 40, 379–408 (2011).
Chakraborty, A. K. & Shakhnovich, E. I. Phase behavior of random copolymers in quenched random media. J. Chem. Phys. 103, 10751–10763 (1995).
Geissler, P. L. & Shakhnovich, E. I. Mechanical response of random heteropolymers. Macromolecules 35, 4429–4436 (2002).
Panganiban, B. et al. Random heteropolymers preserve protein function in foreign environments. Science 359, 1239–1243 (2018).
Koshland, D. E. Jr The key–lock theory and the induced fit theory. Angew. Chem. Int. Ed. Engl. 33, 2375–2378 (1995).
Jayapurna, I. et al. Sequence design of random heteropolymers as protein mimics. Biomacromolecules 24, 652–660 (2023).
Hoshino, T. & Sato, T. Squalene–hopene cyclase: catalytic mechanism and substrate recognition. Chem. Commun. 4, 291–301 (2002).
Moffet, D. A. et al. Peroxidase activity in heme proteins derived from a designed combinatorial library. J. Am. Chem. Soc. 122, 7612–7613 (2000).
Walker, F. A. Models of the bis-histidine-ligated electron-transferring cytochromes. Comparative geometric and electronic structure of low-spin ferro- and ferrihemes. Chem. Rev. 104, 589–616 (2004).
Tronnet, A. et al. Star-like polypeptides as simplified analogues of horseradish peroxidase (HRP) metalloenzymes. Macromol. Biosci. 24, 2400155–2400155 (2024).
Yu, H. et al. Mapping composition evolution through synthesis, purification, and depolymerization of random heteropolymers. J. Am. Chem. Soc. 146, 6178–6188 (2024).
Arbe, A., Colmenero, J., Monkenbusch, M. & Richter, D. Dynamics of glass-forming polymers: “homogeneous” versus “heterogeneous” scenario. Phys. Rev. Lett. 81, 590–593 (1998).
Hart-Cooper, W. M., Clary, K. N., Toste, F. D., Bergman, R. G. & Raymond, K. N. Selective monoterpene-like cyclization reactions achieved by water exclusion from reactive intermediates in a supramolecular catalyst. J. Am. Chem. Soc. 134, 17873–17876 (2012).
Hammer, S. C., Marjanovic, A., Dominicus, J. M., Nestl, B. M. & Hauer, B. Squalene hopene cyclases are protonases for stereoselective Brønsted acid catalysis. Nat. Chem. Biol. 11, 121–126 (2015).
Gibney, B. R. & Dutton, P. L. Histidine placement in de novo–designed heme proteins. Protein Sci. 8, 1888–1898 (1999).
Walker, F. A., Reis, D. & Balke, V. L. Models of the cytochromes b. 5. EPR studies of low-spin iron(III) tetraphenylporphyrins. J. Am. Chem. Soc. 106, 6888–6898 (1984).
Murphy, E. A. et al. High-throughput generation of block copolymer libraries via click chemistry and automated chromatography. Macromolecules 58, 8369–8376 (2025).
Cochran, A. G. & Schultz, P. G. Peroxidase-activity of an antibody heme complex. J. Am. Chem. Soc. 112, 9414–9415 (1990).
Tracy, T. S. Atypical cytochrome P450 kinetics. Drugs R D 7, 349–363 (2006).
Wu, G.-R. et al. Efficient degradation of tetracycline antibiotics by engineered myoglobin with high peroxidase activity. Molecules 27, 8660 (2022).
Jaacks, V. A novel method of determination of reactivity ratios in binary and ternary copolymerizations. Makromolek. Chem. 161, 161–172 (1972).
Flynn, P. F., Mattiello, D. L., Hill, H. D. W. & Wand, A. J. Optimal use of cryogenic probe technology in NMR studies of proteins. J. Am. Chem. Soc. 122, 4823–4824 (2000).
Andreini, C., Cavallaro, G., Lorenzini, S. & Rosato, A. MetalPDB: a database of metal sites in biological macromolecular structures. Nucleic Acids Res. 41, D312–D319 (2013).
Ravel, B. & Newville, M. ATHENA, ARTEMIS, HEPHAESTUS: data analysis for X-ray absorption spectroscopy using IFEFFIT. J. Synchrotron Radiat. 12, 537–541 (2005).
Martínez, L., Andrade, R., Birgin, E. G. & Martínez, J. M. PACKMOL: a package for building initial configurations for molecular dynamics simulations. J. Comput. Chem. 30, 2157–2164 (2009).
Shu, J. Y. et al. Amphiphilic peptide−polymer conjugates based on the coiled-coil helix bundle. Biomacromolecules 11, 1443–1452 (2010).
■ مصدر الخبر الأصلي
نشر لأول مرة على: www.nature.com
تاريخ النشر: 2025-12-31 02:00:00
الكاتب: Hao Yu
تنويه من موقع “yalebnan.org”:
تم جلب هذا المحتوى بشكل آلي من المصدر:
www.nature.com
بتاريخ: 2025-12-31 02:00:00.
الآراء والمعلومات الواردة في هذا المقال لا تعبر بالضرورة عن رأي موقع “yalebnan.org”، والمسؤولية الكاملة تقع على عاتق المصدر الأصلي.
ملاحظة: قد يتم استخدام الترجمة الآلية في بعض الأحيان لتوفير هذا المحتوى.
