Aggregations weak chemical bonds

Fluorinated alcohols are not only interesting as model systems for weak hydrogen bonds with implications in the life sciences [254] and as chemical sensor materials [255], but also provide excellent reaction media [256, 257] and peptide solvents [258 260] with conformation-modulating properties. In both cases, molecular aggregates are thought to play an important role. One of the most widely used fluorinated alcohols is 2,2,2-trifluoroethanol, which will be in the focus of the following section. 

A solution to this problem was proposed in the 1960s by Sidney Fox, on the basis of experimental results that he obtained by heating up a mixture of amino acids in the absence of water. Fox found that, in these conditions, amino acids do aggregate into macromolecules which can even reach large dimensions, and which he called proteinoids. These are not real proteins because their amino acids are not arranged in linear chains of polypeptides, but form directly a variety of three-dimensional chemical bonds. Proteinoids, however, are somewhat similar to proteins in various respects, including a weak catalytic activity (they can, for example, catalyse ATP hydrolysis). 

Aggregation is not solely due to the strong chemical bonds described in Chapter 2. Even noble gas atoms experience weak interatomic forces that lead to liquefaction and, except for helium, solidification at low temperatures. Although these interactions are weak in terms of bond energy, they are of vital importance, especially in living organisms. They also lead to the formation of magnetic domains (Chapter 12) and should not be despised. 

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