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Solubility is the measure of the maximum amount of solute that can be dissolved in a given quantity of solvent at a given temperature and pressure. Solubility is usually measured in molarity (M) or moles per liter (mol/L). A compound is termed soluble if it dissolves in water.
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Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Chȃtelier’s principle. Consider the dissolution of silver iodide:
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Solubility equilibria are established when the dissolution and precipitation of a solute species occur at equal rates. These equilibria underlie many natural and technological processes, ranging from tooth decay to water purification. An understanding of the factors affecting compound solubility is, therefore, essential to the effective management of these processes. This section applies previously introduced equilibrium concepts and tools to systems involving dissolution and precipitation.
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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
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Peptide Solubility Limits: Backbone and Side-Chain Interactions.

Rahul Sarma1, Ka-Yiu Wong1, Gillian C Lynch1

  • 1Sealy Center for Structural Biology and Molecular Biophysics, Department of Biochemistry and Molecular Biology , University of Texas Medical Branch , 301 University Boulevard , Galveston , Texas 77555-0304 , United States.

The Journal of Physical Chemistry. B
|February 1, 2018
PubMed
Summary
This summary is machine-generated.

Pentapeptide solubility in water was simulated, revealing an order matching amino acid monomer solubility. Higher solubility correlates with less time in aggregates and specific interaction dynamics.

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Area of Science:

  • Biochemistry
  • Physical Chemistry
  • Computational Chemistry

Background:

  • Understanding peptide solubility is crucial for various applications.
  • Amino acid monomer solubility provides a reference for peptide behavior.
  • Interactions governing peptide self-assembly are complex.

Purpose of the Study:

  • To determine the solubility limit of pentapeptides in aqueous solutions.
  • To investigate the relationship between peptide solubility and dynamical properties.
  • To elucidate the role of interbackbone interactions in peptide self-assembly.

Main Methods:

  • Simulating phase separation in oversaturated aqueous solutions.
  • Analyzing dynamical properties of peptides, including aggregation behavior.
  • Examining conformational fluctuations and hydration numbers.
  • Investigating energetic mechanisms of interbackbone CO-CO and CO···HN interactions.

Main Results:

  • The solubility limit order of model pentapeptides mirrors experimental amino acid monomer solubility.
  • Peptides with higher solubility spend less time in aggregated clusters.
  • Conformational and hydration fluctuations correlate with peptide solubility.
  • CO-CO interactions are more significant than H-bonds in peptide self-assembly.
  • Interactions involving CO-CO and CO···HN drive the stability of H-bonded peptide pairs.

Conclusions:

  • Peptide solubility is predictable based on amino acid composition and correlates with dynamic behavior.
  • Interbackbone CO-CO interactions play a key role in peptide self-assembly and association.
  • The interplay of CO-CO and CO···HN interactions stabilizes H-bonded peptide pairs.