Towards a 'nano-traffic' system powered by molecular motors

TY - JOUR

T1 - Towards a 'nano-traffic' system powered by molecular motors

AU - Bunk, Richard

AU - Klinth, J

AU - Rosengren, J

AU - Nicholls, I

AU - Tagerud, S

AU - Omling, Pär

AU - Mansson, A

AU - Montelius, Lars

PY - 2003

Y1 - 2003

N2 - In this work, we reconstructed in vitro the behavior of two motor proteins-myosin and actin-responsible for the mechanical action of muscle cells. By transferring this in vivo system to an artificial environment, we were able to study the interaction between the proteins in more detail, as well as investigating the central mechanism of force production. Nm-patterning by e-beam lithography (EBL) could restore parts of the in vivo protein order, essential for potential nanotechnological applications. Much work was put into establishing the necessary compatibility between the biological and nano-lithographical processes. A range of EBL-resists were tested for protein compatibility. One particular kind (MRL-6000.1XP) supported good actin filament motility, while another (PMMA-950) behaved in the opposite way. Taking advantage of these findings, nm-sized lines were created in a double-layer structure of the two resists. The lines were found to act as binding sites for myosin, and as rectifying guides for the linearized motion of actin filaments. Velocities around 5 mum/s were measured. (C) 2003 Elsevier Science B.V. All rights reserved.

AB - In this work, we reconstructed in vitro the behavior of two motor proteins-myosin and actin-responsible for the mechanical action of muscle cells. By transferring this in vivo system to an artificial environment, we were able to study the interaction between the proteins in more detail, as well as investigating the central mechanism of force production. Nm-patterning by e-beam lithography (EBL) could restore parts of the in vivo protein order, essential for potential nanotechnological applications. Much work was put into establishing the necessary compatibility between the biological and nano-lithographical processes. A range of EBL-resists were tested for protein compatibility. One particular kind (MRL-6000.1XP) supported good actin filament motility, while another (PMMA-950) behaved in the opposite way. Taking advantage of these findings, nm-sized lines were created in a double-layer structure of the two resists. The lines were found to act as binding sites for myosin, and as rectifying guides for the linearized motion of actin filaments. Velocities around 5 mum/s were measured. (C) 2003 Elsevier Science B.V. All rights reserved.

KW - actin

KW - lab-on-a-chip

KW - motor proteins

KW - EBL

KW - myosin

U2 - 10.1016/S0167-9317(03)00194-1

DO - 10.1016/S0167-9317(03)00194-1

M3 - Article

VL - 67-8

SP - 899

EP - 904

JO - Microelectronic Engineering

JF - Microelectronic Engineering

SN - 1873-5568

ER -