Fig. 1: Workflow for optimising the solubility of peptides containing modified amino acids (mAAs) using CamSol-PTM.
From: Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids
A linear combination of ALOGPS96,97 and XLOGP3100 is employed to determine the hydrophobicity values. pIChemiSt suite92 is used to predict the pKa values of mAAs. Structural propensities are calculated using a separate predictor that gives an estimate on the likelihood of finding a mAA in an α-helix or a β-sheet. The predictor employs a combination of the number of hydrogen donors and acceptors, the number of rotational bonds, molecular weight and the topological polar surface area. All this information is fed into the CamSol-PTM algorithm to predict the effect of mAAs on the solubility of a peptide.
