title: Increasing protein stability through control of the nanoscale environment.
abstract: We have discovered a novel property of single-walled carbon nanotubes (SWNTs)-their ability to stabilize proteins at elevated temperatures and in organic solvents to a greater extent than conventional flat supports. Experimental results and theoretical analysis reveal that the stabilization results from the curvature of SWNTs, which suppresses unfavorable protein-protein lateral interactions. Our results also indicate that the phenomenon is not unique to SWNTs but could be extended to other nanomaterials. The protein-nanotube conjugates represent a new generation of active and stable catalytic materials with potential use in biosensors, diagnostics, and bioactive films and other hybrid materials that integrate biotic and abiotic components.
authors.affiliation: Department of Chemical and Biological Engineering and Rensselaer Nanotechnology Center, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
authors.forename: Prashanth
authors.initials: P
authors.lastname: Asuri
authors.forename: Sandeep S
authors.initials: SS
authors.lastname: Karajanagi
authors.forename: Hoichang
authors.initials: H
authors.lastname: Yang
authors.forename: Tae-Jin
authors.initials: TJ
authors.lastname: Yim
authors.forename: Ravi S
authors.initials: RS
authors.lastname: Kane
authors.forename: Jonathan S
authors.initials: JS
authors.lastname: Dordick
mesh_terms: D000327:Adsorption; D004355:Drug Stability; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D006108:Graphite; D066298:In Vitro Techniques; D018625:Microscopy, Atomic Force; D008855:Microscopy, Electron, Scanning; D036103:Nanotechnology / Q000379:methods; D037742:Nanotubes, Carbon / Q000737:chemistry* / Q000648:ultrastructure; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
chemical_list: D004800:Enzymes, Immobilized; D037742:Nanotubes, Carbon; D011506:Proteins; D006108:Graphite