Actin motion on microlithographically functionalized myosin surfaces and tracks.
High-resolution e-beam patterning exposure of the surface of poly[(tert-butyl-methacrylate)-co-(methyl methacrylate)]-a common e-beam and deep-UV resist used in semiconductor microlithography-induced sharp changes in the surface hydrophobicity. These differences in hydrophobicity resulted in the selective attachment of heavy meromyosin to hydrophobic, unexposed surfaces. The movement of the actin filaments on myosin-rich and myosin-poor surfaces was statistically characterized in terms of velocity, acceleration, and angle of movement. The actin filaments have a smooth motion on myosin-rich surfaces and an uneven motion on myosin-poor surfaces. Interestingly, an excess of myosin sites has a slowing, albeit mild effect on the motion of the actin filaments. It was also found that the myosin-rich/myosin-poor boundary has an alignment-enforcement effect, especially for the filaments approaching the border from the myosin-rich side. Based on these results, we discuss the feasibility of building purposefully designed molecular motor arrays and the testing of the hypotheses regarding the functioning of the molecular motors.
Nicolau
D V
DV
Osaka National Research Institute, Osaka 563, Japan. dan.nicolau@riotinto.com.au
Suzuki
H
H
Mashiko
S
S
Taguchi
T
T
Yoshikawa
S
S
D000199:Actins / Q000737:chemistry*; D055592:Biophysical Phenomena; D001703:Biophysics; D005453:Fluorescence; D066298:In Vitro Techniques; D020409:Molecular Motor Proteins / Q000737:chemistry; D009038:Motion; D009218:Myosins / Q000737:chemistry*; D019904:Polymethyl Methacrylate; D012666:Semiconductors; D013499:Surface Properties
D000199:Actins; D020409:Molecular Motor Proteins; D019904:Polymethyl Methacrylate; D009218:Myosins