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Determination of the Gas-phase Acidities of Oligopeptides

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Published on: June 24, 2013

ELECTROMETRIC DETERMINATIONS OF THE DISSOCIATION OF GLYCOCOLL AND SIMPLE PEPTIDES.

P H Mitchell¹, J P Greenstein

¹Arnold Biological Laboratory of Brown University, Providence.

The Journal of General Physiology

|October 30, 2009

Summary

This study determined acid-base dissociation constants for various ampholytes, finding they decrease with increased carbon chain length. Results highlight limitations in current solution theories and specific ion effects on constants.

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Area of Science:

Biochemistry
Physical Chemistry

Background:

Ampholytes are molecules with both acidic and basic groups.
Understanding their dissociation constants is crucial for biochemical and chemical applications.

Purpose of the Study:

To determine apparent acid and basic dissociation constants for a series of ampholytes.
To investigate the influence of ionic strength and specific ions (KCl, K2SO4) on these constants.
To discuss the applicability of modern solution theories to ampholytic ions.

Main Methods:

Potentiometric determination using hydrolysis and titration methods.
Measurement of dissociation constants for glycocoll and its derivatives.
Analysis of constants in the presence of KCl and K2SO4 at controlled ionic strength.

Main Results:

Dissociation constants generally decreased as the number of carbon atoms between amino and carboxyl groups increased.
Constants were found to be functions of hydrogen ion activity and solution ionic strength.
Apparent deviations from Debye-Hückel theory were observed and attributed to specific ion effects.

Conclusions:

The electronic structure influences ampholyte dissociation constants.
Current solution theories show inadequacies when applied to ampholytic ions.
Specific ion effects play a significant role in the behavior of ampholytes in solution.