We investigated whether these general observations in AAC would persist regardless of the targeted cancer cell lines. We picked the 11 most evaluated cell lines (Figure ) across different organ tissues; blood (4), brain (1), breast (1), cervix (1), colon (1), lung (2), and prostate (1). We first illustrated the pIC50 values (y) for all mACPs tested against a single cell line (x) where each peptide was labelled as selective (triangle) or non-selective (circle). We also informed how frequently positively or negatively charged residues (Figure ) and small or bulky amino acids (Figure ) were across each mACP. In both figures, ACP-S and ACP-NS displayed pIC50 values across the same range except for HeLa S3, where the ACP-S (triangles) were more potent than their non-selective counterparts (pIC50 ACP-S > 4.7). In Figure , we noted that ACP-S would often contain more small residues (fG,C,A,P,S > 0.0) than their nonselective counterparts (circles) across several cell lines (i.e., U251-MG, NCI-H157, and PC-3). Likewise, we observed non-selective mACPs with higher levels of hydrophobic residues across other cell lines (i.e., Jurkat E6-1, K562) -Figure . We did not report any selective mACP for MDA-MB-361. Both trends indicated that our previous observations about amino acid composition are likely cell line-specific. During that exercise, we noted that peptides would hold constant or varying amino acid compositions across a given range of inhibition for cell lines from one or more organ tissues (e.g., Jurkat E6-1, K562, MDA-MB-361). The cancer cell line HL-60 exhibited a quasi-linear relationship (R 2 =0.66, Figure ) between the peptides' inhibitory activities (pIC50) and their differential enrichments, where the most potent sequences carried multiple positively-charged residues. The relationships between the peptide sequences and their pIC50 values for other cell lines could not be explained solely from their differential enrichments (Figure ).