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Related Concept Videos

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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Adhesion01:14

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Adhesion occurs when one type of molecule is attracted to a different molecule. Water exhibits adhesive properties in the presence of polar surfaces, such as glass or cellulose in plants. For instance, when water is poured into a glass, the positively charged hydrogen molecules of water are more attracted to the negatively charged oxygen molecules in the silica than to the oxygen in neighboring water molecules.
Capillary action is a result of water’s adhesive tendencies. When a narrow...
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Cohesion01:07

Cohesion

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Cohesion is the attraction between molecules of the same type, such as water molecules. Water molecules have an overall neutral charge but are polar molecule. An oxygen atom in one water molecule has a partial negative charge that can bind to a hydrogen atom with a partial positive charge in a second water molecule, forming a hydrogen bond. Each water molecule can form up to four hydrogen bonds with other water molecules. Hydrogen bonds are responsible for water's cohesive nature.
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Surface Tension, Capillary Action, and Viscosity02:57

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Surface Tension
The various IMFs between identical molecules of a substance are examples of cohesive forces. The molecules within a liquid are surrounded by other molecules and are attracted equally in all directions by the cohesive forces within the liquid. However, the molecules on the surface of a liquid are attracted only by about one-half as many molecules. Because of the unbalanced molecular attractions on the surface molecules, liquids contract to form a shape that minimizes the number...
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Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
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Ionic Association01:28

Ionic Association

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The ionic association is the association of oppositely charged ions in an electrolyte solution to form ion pairs. Bjerrum defined ion pairs as two oppositely charged ions whose electrostatic attraction exceeds the thermal energy of the system, typically expressed as 2kT. Electrostatic attraction depends on ionic charge, separation distance, and the dielectric constant of the medium. Thermal energy, represented by kT, reflects the tendency of ions to move independently due to molecular motion.
19

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Probing the Structure and Dynamics of Interfacial Water with Scanning Tunneling Microscopy and Spectroscopy
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Tuning underwater adhesion with cation-π interactions.

Matthew A Gebbie1,2, Wei Wei2, Alex M Schrader2,3

  • 1Materials Department, University of California, Santa Barbara, California 93106, USA.

Nature Chemistry
|April 22, 2017
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Summary
This summary is machine-generated.

Simple peptides with aromatic and lysine residues exhibit strong, reversible adhesion, rivaling marine mussel proteins. Phenylalanine-containing peptides show superior reversible adhesion, demonstrating interfacial confinement

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Area of Science:

  • Biochemistry
  • Materials Science
  • Biomaterials Engineering

Background:

  • Cation-π interactions are crucial for biological molecule self-assembly and cohesion.
  • The energetics of cation-π-driven self-assembly in molecular films are not well understood.
  • Marine mussel adhesion proteins utilize strong reversible intermolecular cohesion.

Purpose of the Study:

  • To investigate the energetics of cation-π-driven self-assembly in simple aromatic- and lysine-rich peptides.
  • To compare the cohesive properties of these peptides with marine mussel adhesion proteins.
  • To explore the impact of interfacial confinement on cation-π-mediated assembly.

Main Methods:

  • Nanoscale force measurements.
  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Analysis of peptide self-assembly and cohesive properties.

Main Results:

  • Simple aromatic- and lysine-rich peptides exhibit cohesive properties comparable to marine mussel adhesion proteins.
  • Peptides containing phenylalanine demonstrate significantly enhanced reversible adhesion interactions.
  • Interfacial confinement fundamentally alters the energetics of cation-π-mediated assembly.

Conclusions:

  • Cation-π interactions in peptides can drive self-assembly and cohesion comparable to natural adhesion proteins.
  • Phenylalanine incorporation enhances reversible adhesion in peptide-based systems.
  • Understanding interfacial confinement effects is key for designing peptide-based biomaterials and rationalizing biological assembly.