Table 1.
Primary and secondary structural comparison of Brevinin-1GHa with relevant antimicrobial peptides (AMPs) homologs
| Peptide Name | Source | Amino Acid Sequence | Alpha Helix | Identities |
|---|---|---|---|---|
| Brevinin-1GHa | Hylarana guentheri |
1FLGAVLKVAGKLVPAAICKISKKC24 chhhhhhhhhhhhhhhhhhhhccc |
83.33% | |
| Brevinin-1HSa | Odorrana hosii |
1FLPAVLRVAAKIVPTVFCAISKKC24 cchhhhhhhhhhccceeeeecccc |
41.67% | 67% |
| Brevinin-1WY7 | Amolops wuyiensis |
47FLGSILGLVGKVVPTLICKISKKC70 cchhhhhhhhhhchheeeeecccc |
50.00% | 67% |
| Brevinin-1WY5 | Amolops wuyiensis |
48FLGSLLGLVGKVVPTLICKISKKC71 chhhhhhhhcccecceeeeeecccc |
29.17% | 67% |
| Brevinin-1JDc | Odorrana jingdongensis |
1FLPAVLRVAAKVVPTVFCLISKKC24 cchhhhhhhhhhccceeeeeeccc |
41.67% | 67% |
| Brevinin-1RTc | Amolops ricketti |
48FLGSLLGLVGKIVPTLICKISKKC71 chhhhhhhhhcecheeeeeecccc |
41.67% | 67% |
| Brevinin-1LTd | Sylvirana latouchii |
48FFGSVLKVAAKVLPAAICQIFKKC71 cchhhhhhhhhhhhhhhhhhhhcc |
83.33% | 67% |
The secondary structures of peptides were predicted by the online HNN program (http://npsa-prabi.ibcp.fr/cgi-bin/npsa_automat.pl?page=/NPSA/npsa_hnn.html). ‘h’ indicates α-helix, ‘c’ indicates random coil and ‘e’ indicates extended strand.