We have used amino acids activated by carbonyldiimidazole to study the enan
tiospecificity of peptide elongation in aqueous solution. Peptide 'primers'
Glu(10) and Ala(3)Glu(10) were elongated with the enantiomers of arginine,
glutamic acid, asparagine, phenylalanine, serine and valine. The homochira
l addition was always the more efficient reaction; the enantiospecificity w
as large in some cases but very small in others. In every case Ala(3)Glu(10
) was elongated more efficiently than Glu(10).