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. 2018 Mar 2;9:329. doi: 10.3389/fmicb.2018.00329

Table 2.

Structure and physicochemical properties of the cationic peptides used in this study.

Alternate name Sequence RP-HPLC MALDI-TOF (M/Z) [M+H]+ bNet charge Residues Hydro-phobic amino acids (%) bGRAVY
atR(Min) Theor. Exper.
Motif 20R R W Q W R25 4.33 985.55 986.66 +3 6 33.3 −3.133
Lineal/palindromic R W Q W R W Q W R 5.95 1,485.75 1,488.58 +3 9 44.4 −2.678
Lfc B reference Peptide 17F K C R R W Q W R M K K L G A31 5.25 1,992.09 1,994.71 +6 15 33.3 −1.207
Dimeric (R R W Q W R)2 K Ahx 5.21 2,195.24 2,198.51 +6 15 26.7
Tetrameric (R R W Q W R)4 K2 Ahx2 C2 19.11 2,298.32c 2,302.96c +12 30 26.7
a

tR: Retention time of the main product (in minutes).

b

Net charge values and Grand Average of Hydropathy (GRAVY) values were calculated using the Antimicrobial Peptide Calculator and Predictor (http://aps.unmc.edu/AP/prediction/prediction_main.php). However, this was not possible for the branched peptides.

c

Experimental molecular weight that correspond to dimeric molecule before oxidation.