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1 October 2000 The Location of Tryptophan, N-acetyltryptophan and α-Chymotrypsin in Reverse Micelles of AOT: A Fluorescence Study
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Abstract

The spectroscopic properties of α-chymotrypsin (α-Chym), l-tryptophan (Trp) and N-acetyl-l-tryptophan (NAT) solubilized in hydrated reverse micelles of sodium bis(2-ethylhexyl) sulfosuccinate in iso-octane were followed by fluorescence as a function of the amount of intramicellar water and initial pH. The lack of pH dependence observed for Trp in these systems, as opposed to what occurs in bulk water, and the similarities found for the protein in both media foresee different locations of these probes. In reverse micelles, fluorescence quenching studies using acrylamide emphasize the existence of structural alterations within the protein when its global charge changes from positive (pH = 7) to negative (pH = 10). The ensemble of the data points to an interfacial location of the zwitterionic Trp, an intermediate region of less tightly bound water for the location of the anionic Trp and NAT and an almost bulk water environment for α-Chym.

Suzana M. Andrade and Sílvia M. B. Costa "The Location of Tryptophan, N-acetyltryptophan and α-Chymotrypsin in Reverse Micelles of AOT: A Fluorescence Study," Photochemistry and Photobiology 72(4), 444-450, (1 October 2000). https://doi.org/10.1562/0031-8655(2000)072<0444:TLOTNA>2.0.CO;2
Received: 14 February 2000; Accepted: 1 June 2000; Published: 1 October 2000
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