↓ Skip to main content

First serine protease inhibitor isolated from Rhinella schneideri poison

Overview of attention for article published in Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
Altmetric Badge

About this Attention Score

  • Average Attention Score compared to outputs of the same age

Mentioned by

twitter
1 tweeter
facebook
1 Facebook page

Citations

dimensions_citation
9 Dimensions

Readers on

mendeley
24 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
First serine protease inhibitor isolated from Rhinella schneideri poison
Published in
Journal of Venomous Animals and Toxins including Tropical Diseases, August 2015
DOI 10.1186/s40409-015-0029-4
Pubmed ID
Authors

Priscila Y T Shibao, Fernando A P Anjolette, Norberto P. Lopes, Eliane C. Arantes

Abstract

Toad secretions are a source of molecules with potential biotechnological application on a wide spectrum of diseases. Toads from the Rhinella family have two kinds of poisonous glands, namely granular and mucous glands. Rhinella schneideri toads produce granular secretions that comprise a great number of molecules, including serine proteases inhibitors. Serine proteases, such as trypsin, chymotrypsin and elastase, are enzymes that have a serine amino acid into its catalytic site and can be found in a large number of vertebrate species and pathogenic microorganisms. Therefore, the present work aims to purify a serine protease inhibitor from Rhinella schneideri granular secretions. This study presents the protocol used to purify a serine protease inhibitor from the Rhinella schneideri poison. The granular secretion was submitted to dialysis in order to separate the low molecular weight compounds, which were submitted to a reversed phase-fast protein liquid chromatography fractionation step in a C2C18 column. The major fractions were tested over trypsin, chymotrypsin and elastase through colorimetric assay. The inhibition tests were performed with the enzyme in absence (positive control) and presence of fractions, denatured enzyme (negative control) and the respective chromogenic substrate. Rs20 was the compound with the major inhibitory activity over chymotrypsin, inducing a delay in the formation of the chromogenic enzymatic product. The structure characterization of Rs20 was performed by high resolution electronspray ionization-mass spectrometry (HRESI-MS) and gas chromatography coupled with mass spectrometry (GC-MS). HRESI showed an intense signal suggesting the presence of bufadienolide with less than 10 ppm error. In addition, it was observed a low intense signal at m/z 399 that could be lithocholic acid, a biosynthetic precursor of bufadienolide. Finally, GC-MS analysis applying NIST library identification reinforced this hypothesis. The current study have isolated and partially characterized the function and structure of the first bufadienolide with inhibitory action over chymotrypsin.

Twitter Demographics

The data shown below were collected from the profile of 1 tweeter who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 24 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Brazil 1 4%
Unknown 23 96%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 6 25%
Researcher 4 17%
Student > Master 3 13%
Student > Postgraduate 2 8%
Student > Ph. D. Student 2 8%
Other 2 8%
Unknown 5 21%
Readers by discipline Count As %
Agricultural and Biological Sciences 7 29%
Pharmacology, Toxicology and Pharmaceutical Science 4 17%
Biochemistry, Genetics and Molecular Biology 4 17%
Economics, Econometrics and Finance 1 4%
Medicine and Dentistry 1 4%
Other 1 4%
Unknown 6 25%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 20 August 2015.
All research outputs
#9,618,589
of 12,526,623 outputs
Outputs from Journal of Venomous Animals and Toxins including Tropical Diseases
#221
of 321 outputs
Outputs of similar age
#149,447
of 237,868 outputs
Outputs of similar age from Journal of Venomous Animals and Toxins including Tropical Diseases
#2
of 3 outputs
Altmetric has tracked 12,526,623 research outputs across all sources so far. This one is in the 19th percentile – i.e., 19% of other outputs scored the same or lower than it.
So far Altmetric has tracked 321 research outputs from this source. They receive a mean Attention Score of 3.3. This one is in the 15th percentile – i.e., 15% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 237,868 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 31st percentile – i.e., 31% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 3 others from the same source and published within six weeks on either side of this one.