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. 2021 Jan 22;11:2132. doi: 10.1038/s41598-021-81734-2

Table 1.

Physiochemical properties and predicted secondary structures of six avian peptides used in this study.

Peptide name Amino acid sequence Length Net charge Mw (Da) pI Hydrophobicity (H) Hydrophobic moment (µM)
CATH-1(6–26) WPLVIRTVIAGYNLYRAIKKK-NH2 21 5 2503 11.02 0.544 0.28
CATH-2(1–15) RFGRFLRKIRRFRPK 15 8 2033 12.81 0.103 0.585
ABD1 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCKRIW 39 8 4510 10 0.547 0.181
ABD2 RDMLFCKGGSCHFGGCPSHLIKVGSCFGFRSCCKWPWNA 39 4 4324 8.38 0.616 0.047
ABD6 SPIHACRYQRGVCIPGPCRWPYYRVGSCGSGLKSCCVRNRWA 42 7 4744 9.43 0.504 0.117
ABD9 DTLACRQSHGSCSFVACRAPSVDIGTCRGGKLKCCKWAPSS 41 4 4288 8.42 0.396 0.094

α-helical structures, random-coil, and extended-strand are indicated as letters h, c, and e, respectively.