Hydrophobic effects history

Certain aspects of the solvent structural changes in regions near to the solute have received specialized attention and even inspired their own nomenclature. Two examples, each with a long and distinguished theoretical history, are the hydrophobic effect and dielectric saturation. ... 

Studies of the association of polyphenols with proteins have a long history (27). Loomis (28) has succinctly summarised the conclusions of this earlier work. The principal means whereby proteins and polyphenols are thought to reversibly complex with one another are (i) hydrogen bonding, (ii) ionic interactions and (iii) hydrophobic interactions. Whilst the major thrust in earlier work was to emphasize the part played by intermolecular hydrogen bonding in the complexation, Hoff (29) has drawn attention to the possibility that hydrophobic effects may dominate the association between the two species. 

An engaging discussion of the history of Benjamin Franklin s experiment and a relatively nontechnical treatment of monolayers and bilayers of surfactants and their implications to biochemistry and biology are presented by Tanford, a pioneer of what is known as the hydrophobic effect and the biological applications of mono- and multilayers (Tanford 1989). Almost all of the material discussed in this highly readable volume is relevant to the focus of this chapter. 

As Tanford (1997) and Tanford and Reynolds (2001) correctly expounded on the history of the hydrophobic effect, the basic ideas of the hydrophobic phenomena were known and discussed long before Kauzmann coined the term hydrophobic bond. Clearly, the HtpO effects are important in processes involving either large numbers of non-polar solutes, or long chain HcpO molecules (such as the formation of micelles and membranes). 

The history of the physicochemical properties of A -acylamino acid started from the patent by Hentrich et al. [27], Since then, Staudinger and Becer reported the solubility and viscosity of A -acylsarcosinate [28] Naudet measured the surface tension and interfacial tension of aqueous solutions of A -acylseri-nate and At-acylleusinate [46], Tsubone measured the surface tension and critical micelle concentration (cmc) of various A -acylamino acids and investigated the effect of structural differences of amino acids and length of fatty acid residue on these surface activities [29], Heitmann [30] further investigated the cmc of Af-acyl cysteine, serine, and glycine and indicated that the-SH in cysteine stabilized the micelle structure with its hydrophobic nature. Ooki reported the surface activities of At-acylsarcosinate [47]. 

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