Characterization of a new bioactive peptide from Potamotrygon gr. orbignyi freshwater stingray venom.
Brazilian freshwater stingrays, Potamotrygon gr. orbigyni, are relatively common in the middle-western regions of Brazil, where they are considered an important public health threat. In order to identify some of their naturally occurring toxin peptides available in very low amounts, we combine analytical protocols such as reversed-phase high-performance liquid chromatography (RP-HPLC), followed by a biological microcirculatory screening and mass spectrometry analysis. Using this approach, one bioactive peptide was identified and characterized, and two analogues were synthesized. The natural peptide named Porflan has the primary structure ESIVRPPPVEAKVEETPE (MW 2006.09 Da) and has no similarity with any bioactive peptide or protein found in public data banks. Bioassay protocols characterized peptides as presenting potent activity in a microcirculatory environment. The primary sequences and bioassay results, including interactions with the membrane phospholipids, suggest that these toxins are a new class of fish toxins, directly involved in the inflammatory processes of a stingray sting.
Conceição
Katia
K
Laboratório Especial de Toxinologia Aplicada, Instituto Butantan, São Paulo, Brazil.
Santos
Juliane M
JM
Bruni
Fernanda M
FM
Klitzke
Clécio F
CF
Marques
Elineide E
EE
Borges
Márcia H
MH
Melo
Robson L
RL
Fernandez
Jorge H
JH
Lopes-Ferreira
Mônica
M
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005397:Fish Venoms / Q000737:chemistry / Q000378:metabolism*; D013058:Mass Spectrometry; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D012860:Skates, Fish / Q000378:metabolism*; D053719:Tandem Mass Spectrometry
D005397:Fish Venoms; D010455:Peptides