Background:
Amphibian skin plays an essential role in protecting organisms from harmful
external factors such as UV radiation. How amphibians protect themselves from reactive oxygen
species following long-term sun exposure is an important and interesting question. Amphibian
skins possess a novel antioxidant system composed of various Antioxidant Peptides (AOPs), which
maintain redox homeostasis. However, only a few AOPs have been identified so far.
Methods:
Using combinational methods of peptidomics and genomics, we characterized a novel
gene-encoded antioxidant peptide (herein named OA-VI12) from Odorrana andersonii skin secretions,
which was produced by the post-translational processing of a 59-residue prepropeptide. The
amino acid sequence of the OA-V112 was 'VIPFLACRPLGL', with a molecular mass of 1298.6 Da
and no observed post-transcriptional modifications. Functional analysis demonstrated that OA-VI12
was capable of scavenging ABTS+, DPPH, NO and decreasing the Fe3+ production.
Results:
We determined that the C7 amino acid was responsible for ABTS+ and Fe3+ scavenging,
activities, the F4, C7, and P9 amino acids were crucial for DPPH scavenging activity, and the P9
amino acid was responsible for NO scavenging activity. Unlike several other amphibian peptides,
OA-VI12 did not accelerate wound healing in a full-thickness skin-wound mouse model and did not
demonstrate direct microbial killing. Here, we identified and named a novel gene-encoded antioxidant
peptide from the skin secretions of an odorous frog species, which may assist in the development
of potential antioxidant candidates.
Conclusion:
This study may help improve our understanding of the molecular basis of amphibians’
adaptation to environments experiencing long-term UV radiation.