title: Biomimicry Promotes the Efficiency of a 10-Step Sequential Enzymatic Reaction on Nanoparticles, Converting Glucose to Lactate.
abstract: For nanobiotechnology to achieve its potential, complex organic-inorganic systems must grow to utilize the sequential functions of multiple biological components. Critical challenges exist: immobilizing enzymes can block substrate-binding sites or prohibit conformational changes, substrate composition can interfere with activity, and multistep reactions risk diffusion of intermediates. As a result, the most complex tethered reaction reported involves only 3 enzymes. Inspired by the oriented immobilization of glycolytic enzymes on the fibrous sheath of mammalian sperm, here we show a complex reaction of 10 enzymes tethered to nanoparticles. Although individual enzyme efficiency was higher in solution, the efficacy of the 10-step pathway measured by conversion of glucose to lactate was significantly higher when tethered. To our knowledge, this is the most complex organic-inorganic system described, and it shows that tethered, multi-step biological pathways can be reconstituted in hybrid systems to carry out functions such as energy production or delivery of molecular cargo.
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Chinatsu
authors.initials: C
authors.lastname: Mukai
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Lizeng
authors.initials: L
authors.lastname: Gao
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Jacquelyn L
authors.initials: JL
authors.lastname: Nelson
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.|Biomedical Engineering, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: James P
authors.initials: JP
authors.lastname: Lata
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Roy
authors.initials: R
authors.lastname: Cohen
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Lauren
authors.initials: L
authors.lastname: Wu
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Meleana M
authors.initials: MM
authors.lastname: Hinchman
authors.affiliation: SUNY Polytechnic Institute, Albany, NY, 12203, USA.
authors.forename: Magnus
authors.initials: M
authors.lastname: Bergkvist
authors.affiliation: LSCLC Proteomics and Mass Spectrometry Facility, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Robert W
authors.initials: RW
authors.lastname: Sherwood
authors.affiliation: LSCLC Proteomics and Mass Spectrometry Facility, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Sheng
authors.initials: S
authors.lastname: Zhang
authors.affiliation: Baker Institute for Animal Health, College of Veterinary Medicine, Cornell University, Ithaca, NY, 14853, USA.|Atkinson Center for a Sustainable Future, Cornell University, Ithaca, NY, 14853, USA.
authors.forename: Alexander J
authors.initials: AJ
authors.lastname: Travis
mesh_terms: D000818:Animals; D000067558:Biological Mimicry; D001709:Biotechnology; D004798:Enzymes / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D005947:Glucose / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D019344:Lactic Acid / Q000737:chemistry / Q000378:metabolism*; D053758:Nanoparticles / Q000737:chemistry / Q000378:metabolism*; D036103:Nanotechnology
chemical_list: D004798:Enzymes; D004800:Enzymes, Immobilized; D019344:Lactic Acid; D005947:Glucose
keywords: biomimicry; enzymes; glycolysis; nanoparticles; tethered enzymes