Dataset Information

Human serum interactome of snake-derived antimicrobial peptide Ctn[15-34]

ABSTRACT: The affinity purification/MS identification methodology reported here can be viewed as a routine pharmacoproteomic approach to investigate the serum interactome of peptide drugs, identifying proteins affecting bioavailability and thus assisting the peptide drug development process. The specific results described here enlighten the serum stability issues of peptide Ctn[15-34] and ratifiy its promising future as an anti-infective lead.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Serum

SUBMITTER: Clara Pérez-Peinado

LAB HEAD: David Andreu

PROVIDER: PXD013425 | Pride | 2019-05-06

REPOSITORIES: Pride

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Publications

Decoding the human serum interactome of snake-derived antimicrobial peptide Ctn[15-34]: Toward an explanation for unusually long half-life.

Pérez-Peinado Clara C Defaus Sira S Sans-Comerma Laura L Valle Javier J Andreu David D

Journal of proteomics 20190430

The inherent propensity to enzymatic degradation of most peptides remains a bottleneck in their therapeutic development. Efficient, early screening methods are necessary for in vitro characterization of the molecular events occurring when peptides get in contact with biological fluids such us plasma. Herein we present an affinity purification/MS approach for mapping peptide serum interactors. We have applied this methodology to identify the serum partners of antibiotic peptide Ctn [15-34], aimin ...[more]

PMID: 31051282

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Project description:Bothrops moojeni has a wide distribution in Brazil and represents a serious medical concern at some localities. Previous works reported that the manifestations of snakebites caused by B. moojeni juveniles were mainly related to coagulation, while those caused by adults had more prominent local damage. In this work, we aimed to analyze the venoms of B. moojeni at different life stages to better understand how the venom shifts along the ontogeny. Snakes were grouped by age and sex, and venom pools were formed accordingly. Compositional analyses by one-dimensional electrophoresis (1-DE), chromatography and mass spectrometry revealed that ontogenetic changes may be mostly related to phospholipase A2 (PLA2) and metalloproteases. Regarding the functional aspect of the venoms, in vitro assays of proteolytic, L-amino acid oxidase, PLA2 and coagulant activities were assayed, but only the first and the last showed age-related changes, with the venom of younger snakes displaying lower proteolytic and higher coagulant activities up to 1 year-old; from 2 years-old onward, the venoms presented the opposite relation. The venoms of 3 years-old snakes were exceptions to the compositional and functional pattern of adults. Sex-related differences were observed at specific groups and not related to age. In vivo experiments (median lethal dose and hemorrhagic activity) were statistically similar between neonates and adults, but observation of the time each venom took to kill the mice revealed that the adult one seemed to act faster than the venoms of the neonates. All venoms were mostly recognized by the antibothropic serum and displayed similar profiles to 1-DE in western blotting. In conclusion, the venoms showed ontogenetic shift in composition and activities. Furthermore, this change occurred from 1 to 2 years-old, and interestingly the 3 years-old pools had particular characteristics, which highlight the importance of extending the studies to better understand venom variability.

			Action	DRS
	Control1.msf	Msf
	Control1.raw	Raw
	Control2.msf	Msf
	Control2.raw	Raw
	Control3.msf	Msf