Abstract
Liver-expressed antimicrobial peptide 2 (LEAP2) is the second blood-derived peptide identified from human blood and shows antimicrobial activity and predominant expression in the liver. It is a cysteine-rich antimicrobial peptide characterized by the presence of a four cystein conserved motifs and two intracellular disulphide bridges. In silico analyses of avian LEAP2 sequences were performed in the study. Mature peptide regions were found to be highly conserved in comparison to pro-domain and signal sequence. Majority of the avian samples analyzed possessed RQRR motif at the cleavage site between pro-region and mature region. Beyond microbial killing, LEAP2 of Aquila chrysaetos canadensis has been found to play additional roles in signaling pathway, oocyte, follicular development, cytokine activity and in apoptosis regulation. Higher conservation in the amino acid sequences of LEAP2 among birds suggests the significant role of this molecule in avian evolution.
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