Effect of positional environmental domains on the variation of high-performance liquid chromatographic peptide retention coefficients.

While attempting to derive a set of high-performance liquid chromatographic amino acid retention coefficients from a set of 298 related peptide analogues of a 13-amino acid peptide, we found that each position within the peptide would require a different set of retention coefficients to accurately predict peptide retention times. Furthermore, our results show that peptides having the same amino composition but slightly different sequences can have very different retention times. We believe that individual sequence domains and the resulting differences in the solid phase-mobile phase interactions must be taken into account for the accurate prediction of peptide retention times.

Simplified procedure for carrying out simultaneous multiple hydrogen fluoride cleavages of protected peptide resins.

Methods have recently been presented which greatly increase the ability to synthesize large numbers of peptides. These advances make it essential to be able to cleave large numbers of protected peptide resins. Two different procedures are presented for carrying out cleavage of protected peptide resins. The first procedure enables multiple cleavages to be carried out with many existing HF apparatuses, while the second utilizes a new apparatus design. Using these procedures, at least 50 individual cleavages can be carried out per day.