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Journal of Bioactive and Compatible Polymers
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Oligopeptides as an Oral Delivery System II. Effect of Amino Acid Sequences on Aggregation Behavior

Mamoru Haratake

Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284-2006

Ruifeng Zhao

Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284-2006

Raphael M. Ottenbrite

Department of Chemistry, Virginia Commonwealth University, Richmond, VA 23284-2006

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.

Journal of Bioactive and Compatible Polymers, Vol. 12, No. 4, 282-293 (1997)
DOI: 10.1177/088391159701200402
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