Unusually stable β‐sheet formation in an ionic self‐complementary oligopeptide

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Abstract
A 16‐residue amphiphilic oligopeptide (EAK16) with every other residue alanine and also containing glutamic acid and lysine (Ac‐NH‐AEAEAKAKAEAEAKAK‐CONH2) is able to form an unusually stable β‐sheet structure. The β‐sheet structure is stable at very low concentrations in water and at high temperatures. Various pH changes at 1.5, 3, 7, and 11 had little effect on the stability of the β‐sheet structure. The β‐sheet structure was not altered significantly even in the presence of 0.1% SDS, 7 molar guanidine hydrochloride, or 8 molar urea. One of the structural characteristics of the EAK16 is its ionic self‐complementarity in that ionic bonds and hydrogen bonds between Glu and Lys can form readily between two oligopeptide β‐sheet structures. This structural feature is probably one of the factors that promotes its extreme stability. This is the first example of such an extended ionic self‐complementarity in a protein structure. EAK16 and its related peptides may have applications as useful biomaterials. It also offers a good model for studying the mechanism of β‐sheet formation. Because the oligopeptide can self‐assemble to form a membranous structure, it may have relevance to origin of life research. © 1994 John Wiley & Sons, Inc.