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Compartmentalization of amino acids in surfactant aggregates - Partitioning between water and aqueous micellar sodium dodecanoate and between hexane and dodecylammonium propionate trapped water in hexaneThe partitioning of amino acids (glycine, alanine, leucine, phenylalanine, histidine, aspartic acid, glutamic acid, lysine, isoleucine, threonine, serine, valine, proline, arginine) in aqueous and nonaqueous micellar systems was studied experimentally. Partitioning from neat hexane into dodecylammonium propionate trapped water in hexane was found to be dependent on both electrostatic and hydrophobic interactions, which implies that the interior of dodecylammonium propionate aggregates is negatively charged and is capable of hydrogen bonding in addition to providing a hydrophobic environment. Unitary free energies of transfer of amino acid side chains from hexane to water were determined and solubilities of amino acids in neat hexane substantiated the amino acid hydrophobicity scale. The relevance of the experiments to prebiotic chemistry was examined.
Document ID
19760057169
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Fendler, J. H.
(Texas A&M Univ. College Station, TX, United States)
Nome, F.
(Texas A&M Univ. College Station, TX, United States)
Nagyvary, J.
(Texas A & M University College Station, Tex., United States)
Date Acquired
August 8, 2013
Publication Date
November 4, 1975
Publication Information
Publication: Journal of Molecular Evolution
Volume: 6
Subject Category
Life Sciences (General)
Accession Number
76A40135
Distribution Limits
Public
Copyright
Other

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