| Abstract
| - On the basis of suggestive X-ray data, 14 aroyl l-cystine derivatives were designed, synthesized,and examined for their ability to gelate water. Several members of this amino acid family are remarkablyeffective aqueous gelators (the best being one that can rigidify aqueous solutions at 0.25 mM, ca. 0.01%, inless than 30 s!). A few of the analogues separate from water as crystals, indicating a close relationship betweengelation and crystallization. All effective gelators self-assemble into fibrous structures that entrain the solventin the capillary spaces among them. Hydrogen-bonding sites on the compounds that might stabilize the fiberswere identified from specific substitutions that replace a hydrogen donor with a methyl group, enhance thehydrogen-accepting ability of a carbonyl oxygen, or promote the hydrogen-donating ability of an amide proton.The structural variations were characterized via minimal gelation concentrations and times, X-ray crystallography,light and electron microscopy, rheology, and calorimetry. The multiple techniques, applied to the diversecompounds, allowed an extensive search into the basis of gelation. It was learned, for example, that the compoundwith the lowest minimum gelator concentration and time also has one of the weakest gels (i.e., it has a lowelastic modulus). This is attributed to kinetic effects that perturb the length of the fibers. It was also arguedthat π/π stacking, the carboxyl carbonyl (but not the carboxyl proton), and solubility factors all contribute tothe stability of a fiber. Polymorphism also plays a role. Rheological studies at different temperatures showthat certain gels are stable to a 1-Hz, 3-Pa oscillating shear stress at temperatures as high as 90 °C. Other gelshave a “catastrophic” break at lower temperatures. Calorimetric data indicate a smooth transition from gel tosol as the temperature is increased. These and other issues are discussed in this “anatomy” of a gel.
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