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. 2020 Aug 6;9(8):209. doi: 10.3390/biology9080209

Table 1.

The physicochemical properties of Brevinin-1 peptides and B1A’s analogues.

Peptide Sequences Residue No Charge Hydrophobicity <H> Hydrophobic moment <µH>
B1PLB FLPLIAGLAANFLPKIFCAITKKC 24 3 0.834 0.310
B1PLC FLPVIAGVAAKFLPKIFCAITKKC 24 4 0.778 0.352
B1A FLPLIAGLAAKFLPKIFCAITKKC 24 4 0.818 0.326
B1A1 FLPLIAGLAAKCAITKKC 18 3 0.712 0.246
B1A2 FLPKIFCAITKKC 13 3 0.791 0.552
KB2 KFLPKIFCAITKKC 14 4 0.644 0.577
KKB2 KKFLPKIFCAITKKC 15 5 0.553 0.505
KWB2 KFLPWKIFCAITKKC 15 4 0.789 0.285
KKWB2 KKFLPWKIFCAITKKC 16 5 0.659 0.255
KW3,5B2 KFWPWKIFCAITKKC 15 4 0.806 0.263
KW5,7B2 KFLPWKWFCAITKKC 15 4 0.799 0.287