Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Selective spatial localization of actomyosin motor function by chemical surface patterning.

Mark Sundberg1, Martina Balaz, Richard Bunk

  • 1Department of Chemistry and Biomedical Sciences, University of Kalmar, SE-39182 Kalmar, Sweden.

Langmuir : the ACS Journal of Surfaces and Colloids
|August 9, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Design of Hyperporous Molecularly Imprinted Thin Films for Ultrasensitive Antibody-Free QCM Detection of a Small-Cell Lung Cancer Biomarker.

ACS sensors·2026
Same author

Editorial: Release of inorganic phosphate from the myosin active site in actomyosin energy transduction.

Frontiers in physiology·2026
Same author

Temperature-Assisted Gas-phase Silanization Using Different Silanes for Actomyosin-Based Nanodevices.

ACS omega·2026
Same author

Kolbe radical-initiated electrochemical desulfurization of thioamides under aerobic conditions.

Chemical communications (Cambridge, England)·2026
Same author

Recent Advancements in Nickel-Catalyzed Electrochemical Reductive Cross-Coupling.

ACS organic & inorganic Au·2025
Same author

A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.

Frontiers in physiology·2025

Heavy meromyosin (HMM) drives actin filament sliding on trimethylchlorosilane (TMCS) surfaces, with higher velocity than on glass or silicon dioxide (SiO2). This motility is selective, with HMM binding hindering actin on SiO2/glass.

Area of Science:

  • Biophysics
  • Materials Science
  • Cell Biology

Background:

  • Previous work demonstrated actin filament guidance and sliding on nanosized tracks with adsorbed heavy meromyosin (HMM).
  • Tracks were previously functionalized with trimethylchlorosilane (TMCS) via chemical vapor deposition (CVD) and surrounded by hydrophilic areas.

Purpose of the Study:

  • To evaluate the quality of HMM function on CVD-TMCS surfaces compared to standard nitrocellulose.
  • To investigate the influence of surface physical and buffer chemical properties on HMM-induced actin motility.
  • To determine the motility selectivity between different surface chemistries (TMCS vs. glass/SiO2).

Main Methods:

  • In vitro motility assays on nonpatterned and patterned surfaces (micro- and nano-).
  • Surface characterization using contact angle measurements.

Related Experiment Videos

  • Biochemical assays including HMM depletion spectrophotometry, K/EDTA ATPase activity, and total internal reflection fluorescence spectroscopy (TIR-F).

    • Main Results:

    • HMM function quality on CVD-TMCS is equivalent to standard nitrocellulose.
    • Methylcellulose addition enabled HMM-induced actin sliding on both glass/SiO2 and TMCS, with higher velocity on TMCS.
    • Actin motility was observed on TMCS but not on glass/SiO2 in the absence of methylcellulose, demonstrating complete motility selectivity.

    Conclusions:

    • Surface chemistry significantly impacts HMM-actin interaction and motility.
    • TMCS surfaces support high-quality actin motility, while glass/SiO2 surfaces hinder it, despite similar HMM surface densities.
    • The observed motility contrast is attributed to different HMM binding modes affecting actin binding on SiO2/glass.