Abstract
The effect of amino acid sequences on the aggregation and the subsequent sphere formation behavior of tetrapeptides, pEE(a)X(y) involving glutamic acid (E), phenylalanine (F), tyrosine (Y), alanine (A), and leucine (L) were investigated by light scattering and light microscopy. At 0.1 M pEE(a)Y(y)Y and pEE(a)F(y)F showed similar pH and concentration-dependent aggregation behaviors. These tetrapeptides also showed similar aggregation profiles in the presence of macromolecular drugs. Only pEE(a)F(y)F produced discrete spheres in the presence of protein drugs. Neither pEE(a)A(y)A nor pEE(a)L(y)L gave aggregates even at 0.1 M at pH 2. Consequently, the amino acids terminal positions are important in the aggregation characteristics of the tetrapeptides.
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