Our MinHashed fingerprints performed very well with peptide stereoisomers. In the case of the antimicrobial undecapeptide ln65 (7), a membrane disruptive antimicrobial peptide whose activity/toxicity balance is modulated by stereochemical variations and which motivated the present study, the three chiral MAP fingerprints distinguished all the 2,048 possible stereoisomers. By contrast, ECFP6C only saw about half of them and ECFP4C and APC distinguished less than 10%, most likely because this peptide is composed of only lysine and leucine residues, which reduces the number of possible substructures. The chiral MAP fingerprints also distinguished the 330 possible sequence-scrambled isomers of 7 and the 675,840 possible stereoisomers of sequence-scrambled isomers of 7. By comparison, APC succeeded for the 330 scrambled sequences but failed on the larger set, and both chiral ECFPs failed in both cases, which can be attributed to the absence of long-range substructures in ECFP fingerprints.