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

Fibrous long spacing collagen ultrastructure elucidated by atomic force microscopy

M F Paige1, J K Rainey, M C Goh

  • 1Department of Chemistry, University of Toronto, Ontario, Canada.

Biophysical Journal
|June 23, 1998
PubMed
Summary

Researchers created fibrous long spacing (FLS) collagen fibrils in vitro, observing their unique structure and assembly mechanism using atomic force microscopy. These FLS fibrils exhibit distinct banding and protofibril arrangements, differing from native collagen.

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

A novel sample holder allowing atomic force microscopy on transmission electron microscopy specimen grids: repetitive, direct correlation between AFM and TEM images.

Journal of microscopy·2002
Same author

A study of fibrous long spacing collagen ultrastructure and assembly by atomic force microscopy.

Micron (Oxford, England : 1993)·2000
Same author

Ultrastructure and assembly of segmental long spacing collagen studied by atomic force microscopy.

Micron (Oxford, England : 1993)·2000
Same author

Paired helical filaments are twisted ribbons composed of two parallel and aligned components: image reconstruction and modeling of filament structure using atomic force microscopy.

Journal of neuropathology and experimental neurology·1997
Same author

Sequential assembly of collagen revealed by atomic force microscopy.

Biophysical journal·1995
Same author

Alzheimer paired helical filaments: a comparison with the twisted ribbon model.

Acta neuropathologica·1995

Area of Science:

  • Biomaterials Science
  • Structural Biology
  • Biophysics

Background:

  • Native collagen exhibits a characteristic 67-nm periodicity.
  • Fibrous long spacing (FLS) collagen fibrils present a periodicity greater than native collagen.
  • Understanding collagen fibril assembly is crucial for biomaterial development.

Purpose of the Study:

  • To characterize the in vitro formation and ultrastructure of fibrous long spacing (FLS) collagen fibrils.
  • To investigate the assembly mechanism of FLS fibrils.
  • To compare the structure and assembly of FLS fibrils with native collagen.

Main Methods:

  • In vitro self-assembly of collagen fibrils using alpha1-acid glycoprotein.
  • Atomic force microscopy (AFM) for high-resolution imaging of fibril structure.

Related Experiment Videos

  • Comparative analysis of FLS and native collagen fibril morphology.

    • Main Results:

    • FLS fibrils were successfully formed in vitro, with diameters around 150 nm.
    • A distinct banding pattern with 250-nm periodicity was observed in FLS fibrils.
    • Ultrastructural analysis revealed aligned protofibrils forming grooves (2 nm deep, 20 nm wide) on FLS fibrils.
    • FLS fibril growth appears to involve protofibril merging, entanglement, and packing.

    Conclusions:

    • Fibrous long spacing collagen fibrils can be formed in vitro under specific conditions.
    • The assembly mechanism of FLS fibrils involves protofibril organization and packing.
    • FLS fibrils possess a unique ultrastructure and assembly pathway distinct from native collagen.