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 Concept Videos

Atomic Force Microscopy01:08

Atomic Force Microscopy

4.6K
Atomic force microscopy (AFM) is a type of scanning probe microscopy that can analyze topographic details of various specimens like ceramics, glass, polymers, and biological samples. AFM offers over 1000 times more resolution than the optical imaging system. Images generated from AFM are three-dimensional surface profiles, offering an advantage over the flat, two-dimensional images from other imaging techniques.
The AFM Probe
The probe is regarded as the heart of any AFM setup and comprises the...
4.6K
Amyloid Fibrils03:03

Amyloid Fibrils

12.1K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
12.1K
Intermolecular Forces03:13

Intermolecular Forces

72.4K
Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen...
72.4K
Intermolecular vs Intramolecular Forces03:00

Intermolecular vs Intramolecular Forces

98.0K
Intermolecular forces (IMF) are electrostatic attractions arising from charge-charge interactions between molecules. The strength of the intermolecular force is influenced by the distance of separation between molecules. The forces significantly affect the interactions in solids and liquids, where the molecules are close together. In gases, IMFs become important only under high-pressure conditions (due to the proximity of gas molecules). Intermolecular forces dictate the physical properties of...
98.0K
The Energies of Atomic Orbitals03:21

The Energies of Atomic Orbitals

30.3K
In an atom, the negatively charged electrons are attracted to the positively charged nucleus. In a multielectron atom, electron-electron repulsions are also observed. The attractive and repulsive forces are dependent on the distance between the particles, as well as the sign and magnitude of the charges on the individual particles. When the charges on the particles are opposite, they attract each other. If both particles have the same charge, they repel each other.
30.3K
Atomic Orbitals02:44

Atomic Orbitals

45.3K
An atomic orbital represents the three-dimensional regions in an atom where an electron has the highest probability to reside. The radial distribution function indicates the total probability of finding an electron within the thin shell at a distance r from the nucleus. The atomic orbitals have distinct shapes which are determined by l, the angular momentum quantum number. The orbitals are often drawn with a boundary surface, enclosing densest regions of the cloud.
45.3K

You might also read

Related Articles

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

Sort by
Same author

Clinical effectiveness and safety of laser lancing for heel puncture in preterm infants: a randomized crossover non-inferiority trial.

Journal of perinatology : official journal of the California Perinatal Association·2026
Same author

Rethinking surgical strategy for margin-positive only T1 colorectal cancer: a multicenter retrospective cohort study.

International journal of colorectal disease·2026
Same author

Compartment-Specific Immune Remodeling of Renal Aging With C1q-Associated Podocyte Activation.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2026
Same author

M-CSF priming enhances the efficiency and reproducibility of hiPSC-derived osteoclast differentiation and pharmacological responsiveness to anti-resorptive agents.

Scientific reports·2026
Same author

Laboratory Assessment and Clinical Outlook for <i>Ex Vivo</i>-Produced Human Platelets and Megakaryocytes from Stem Cell Sources.

Annals of laboratory medicine·2026
Same author

PMSA as a potential modulator of calcineurin phosphatase activity.

Scientific reports·2026

Related Experiment Video

Updated: Feb 14, 2026

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

12.2K

Probing Amyloid β and the Antibody Interaction Using Atomic Force Microscopy.

Sung-Woong Han1, Tae-Hoon Lee2, Min-Sik Kang1

  • 1National Institute for Nanomaterials Technology, Pohang University of Science and Technology, 77, Cheongam-ro, Nam-gu, Pohang, Gyeongbuk, 37673, Korea.

Journal of Nanoscience and Nanotechnology
|February 17, 2018
PubMed
Summary

Researchers used atomic force microscopy to study Alzheimer's disease (AD) amyloid-beta (Aβ) interactions with antibodies. Antibody42 demonstrated a significantly longer bond lifetime with Aβ, suggesting its superiority for developing Aβ sensors.

More Related Videos

Bacterial Immobilization for Imaging by Atomic Force Microscopy
10:03

Bacterial Immobilization for Imaging by Atomic Force Microscopy

Published on: August 10, 2011

17.9K
Correlative Light and Electron Microscopy to Study Microglial Interactions with &#946;-Amyloid Plaques
10:52

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques

Published on: June 1, 2016

12.0K

Related Experiment Videos

Last Updated: Feb 14, 2026

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
09:52

Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging

Published on: January 31, 2019

12.2K
Bacterial Immobilization for Imaging by Atomic Force Microscopy
10:03

Bacterial Immobilization for Imaging by Atomic Force Microscopy

Published on: August 10, 2011

17.9K
Correlative Light and Electron Microscopy to Study Microglial Interactions with &#946;-Amyloid Plaques
10:52

Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques

Published on: June 1, 2016

12.0K

Area of Science:

  • Biochemistry
  • Neuroscience
  • Biophysics

Background:

  • Alzheimer's disease (AD) is characterized by amyloid-beta (Aβ) plaque accumulation.
  • Aβ peptide's role in neurotoxicity and AD pathogenesis is critical.
  • Understanding Aβ-antibody interactions is key for diagnostic and therapeutic development.

Purpose of the Study:

  • To investigate the molecular interactions between amyloid-beta (Aβ) and specific antibodies.
  • To compare the binding characteristics of two distinct antibodies targeting Aβ.
  • To evaluate the potential of these antibodies for developing Aβ sensors.

Main Methods:

  • Utilized atomic force microscopy (AFM) to probe Aβ-antibody interactions at the single-molecule level.
  • Employed single molecular force spectroscopy (SMFS) for quantitative binding analysis.
  • Modified AFM probes and glass substrates with specific antibodies and Aβ peptides, respectively.

Main Results:

  • Quantified the dissociation constants for single Aβ-antibody42 and Aβ-antibody16 interactions.
  • Determined a dissociation constant of 5.2 × 10⁻³ s⁻¹ for Aβ-antibody42.
  • Found that Aβ-antibody42 exhibited a 5.3 times longer bond lifetime compared to Aβ-antibody16.

Conclusions:

  • Antibody42 demonstrates superior binding kinetics and stability with Aβ compared to antibody16.
  • The findings suggest antibody42 is a more suitable candidate for the development of sensitive Aβ sensors.
  • This research provides valuable insights into Aβ-antibody interactions for Alzheimer's disease research.