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Sökning: WFRF:(Tagerud S) > (2003) > Towards a 'nano-tra...

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

Bunk, Richard (författare)
Lund University,Lunds universitet,Fasta tillståndets fysik,Fysiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Solid State Physics,Department of Physics,Departments at LTH,Faculty of Engineering, LTH
Klinth, J (författare)
Rosengren, J (författare)
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Nicholls, I (författare)
Tagerud, S (författare)
Omling, Pär (författare)
Lund University,Lunds universitet,Fasta tillståndets fysik,Fysiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Solid State Physics,Department of Physics,Departments at LTH,Faculty of Engineering, LTH
Mansson, A (författare)
Montelius, Lars (författare)
Lund University,Lunds universitet,Fasta tillståndets fysik,Fysiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Solid State Physics,Department of Physics,Departments at LTH,Faculty of Engineering, LTH
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 (creator_code:org_t)
2003
2003
Engelska.
Ingår i: Microelectronic Engineering. - 1873-5568. ; 67-8, s. 899-904
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • 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.

Ämnesord

NATURVETENSKAP  -- Fysik -- Den kondenserade materiens fysik (hsv//swe)
NATURAL SCIENCES  -- Physical Sciences -- Condensed Matter Physics (hsv//eng)

Nyckelord

actin
lab-on-a-chip
motor proteins
EBL
myosin

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