TY - JOUR
T1 - De novo sequencing of peptides from the parotid secretion of the cane toad, Bufo marinus (Rhinella marina)
AU - Rash, Lachlan D.
AU - Morales, Rodrigo A.V.
AU - Vink, Simone
AU - Alewood, Paul F
PY - 2011/2
Y1 - 2011/2
N2 - Amphibian skin secretions are well known as a rich source of bioactive peptides. However, little is known about the presence or role of peptides in the highly toxic, parotid secretion of the cane toad or giant toad, Bufo marinus (Rhinella marina), though small molecule bufadienolides, which act as potent cardiotoxins, have been described. In the current study we used RP-HPLC, MALDI-TOF mass spectrometry and tandem mass spectrometry to analyze and determine the first sequences of peptides from the parotid secretion of B. marinus. We show that peptides in the range of 900-2500 Da are indeed present, however in extremely low abundance. Despite the low abundance, the sequences of 14 peptides were determined, several of which match fragments of larger cellular proteins, yet none share substantial homology with defensive or anti-microbial peptides reported from frog skin secretions. We conclude that peptides are present in the parotid glands of B. marinus only in very low quantities and that they are likely to be breakdown products of proteins involved in cell maintenance. Given these results, we conclude that peptides are unlikely to contribute directly to the high toxicity of the cane toad.
AB - Amphibian skin secretions are well known as a rich source of bioactive peptides. However, little is known about the presence or role of peptides in the highly toxic, parotid secretion of the cane toad or giant toad, Bufo marinus (Rhinella marina), though small molecule bufadienolides, which act as potent cardiotoxins, have been described. In the current study we used RP-HPLC, MALDI-TOF mass spectrometry and tandem mass spectrometry to analyze and determine the first sequences of peptides from the parotid secretion of B. marinus. We show that peptides in the range of 900-2500 Da are indeed present, however in extremely low abundance. Despite the low abundance, the sequences of 14 peptides were determined, several of which match fragments of larger cellular proteins, yet none share substantial homology with defensive or anti-microbial peptides reported from frog skin secretions. We conclude that peptides are present in the parotid glands of B. marinus only in very low quantities and that they are likely to be breakdown products of proteins involved in cell maintenance. Given these results, we conclude that peptides are unlikely to contribute directly to the high toxicity of the cane toad.
KW - De novo sequencing
KW - MALDI-TOF MS/MS
KW - Parotid secretion
KW - Peptide
KW - Rhinella marina
UR - http://www.scopus.com/inward/record.url?scp=79251617941&partnerID=8YFLogxK
U2 - 10.1016/j.toxicon.2010.11.012
DO - 10.1016/j.toxicon.2010.11.012
M3 - Article
C2 - 21115026
AN - SCOPUS:79251617941
SN - 0041-0101
VL - 57
SP - 208
EP - 216
JO - Toxicon
JF - Toxicon
IS - 2
ER -