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Related Concept Videos

Intermolecular Forces in Solutions02:28

Intermolecular Forces in Solutions

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The formation of a solution is an example of a spontaneous process, a process that occurs under specified conditions without energy from some external source.
When the strengths of the intermolecular forces of attraction between solute and solvent species in a solution are no different than those present in the separated components, the solution is formed with no accompanying energy change. Such a solution is called an ideal solution. A mixture of ideal gases (or gases such as helium and argon,...
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Intermolecular Forces03:13

Intermolecular Forces

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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...
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Intermolecular vs Intramolecular Forces03:00

Intermolecular vs Intramolecular Forces

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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...
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Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, and solubilities (miscibilities) of substances. Molar mass, molecular shape, and polarity affect the strength of different intermolecular forces, which influence the magnitude of physical properties across a family of molecules.
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Amyloid Fibrils03:03

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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. 
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Polymers02:34

Polymers

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The word polymer is derived from the Greek words “poly” which means “many” and “mer” which means “parts”. Polymers are long chains of molecules composed of repeating units of smaller molecules, known as monomers. They either occur naturally, such as DNA and proteins, or can be constructed synthetically, like plastics. They have varied structural characteristics, such as linear chains, branched chains, or complex networks, that contribute to the...
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Related Experiment Video

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Correlative Light and Electron Microscopy to Study Microglial Interactions with β-Amyloid Plaques
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Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.

Sibaprasad Maity1, Apurba Pramanik1, Yuri L Lyubchenko1

  • 1Department of Pharmaceutical Sciences , University of Nebraska Medical Center , 986025 Nebraska Medical Center , Omaha , Nebraska 68198 , United States.

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Researchers developed a new method to study amyloid-beta trimers, crucial in Alzheimer's disease. This technique reveals stepwise dissociation, offering insights into toxic protein aggregate formation.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Amyloid oligomers are key neurotoxic species in protein aggregation disorders like Alzheimer's disease.
  • Characterizing transient amyloid oligomers, such as amyloid-beta (Aβ) peptide aggregates, is challenging.
  • Previous work established a flexible nanoarray (FNA) method for probing Aβ (14-23) dimers.

Purpose of the Study:

  • To modify and enhance the FNA method for assembling and probing Aβ (14-23) trimers.
  • To characterize the structural and dynamic properties of Aβ (14-23) trimers.
  • To investigate the dissociation mechanisms of Aβ (14-23) trimers.

Main Methods:

  • Incorporation of dibenzocyclooctyne (DBCO) groups onto an FNA template for metal-free click chemistry.
  • Assembly of Aβ (14-23) monomers onto the functionalized FNA template via click chemistry.
  • Atomic force microscopy (AFM) force spectroscopy to measure dissociation forces of the assembled trimers.

Main Results:

  • Successful assembly and characterization of Aβ (14-23) trimers using the enhanced FNA method.
  • Stepwise dissociation of the trimer was observed, with distinct rupture forces for monomer and dimer dissociation.
  • The first monomer dissociation occurred at ~48 ± 2.4 pN, followed by dimer dissociation at ~53 ± 3.2 pN.
  • The assembled trimers exhibited dynamic behavior, with transient species identified.

Conclusions:

  • The enhanced FNA method provides a robust platform for studying transient amyloid oligomers.
  • Aβ (14-23) trimers exhibit a stepwise dissociation mechanism, providing insights into aggregate stability.
  • The dynamic nature of these trimers highlights the complexity of protein aggregation in neurodegenerative diseases.