Next Article in Journal
Antibacterial and Cytotoxic New Napyradiomycins from the Marine-Derived Streptomyces sp. SCSIO 10428
Next Article in Special Issue
Conopeptides from Cape Verde Conus crotchii
Previous Article in Journal
Bioactive Phenylalanine Derivatives and Cytochalasins from the Soft Coral-Derived Fungus, Aspergillus elegans
Previous Article in Special Issue
Antifreeze Peptides and Glycopeptides, and Their Derivatives: Potential Uses in Biotechnology
Article Menu

Export Article

Open AccessReview
Mar. Drugs 2013, 11(6), 2069-2112; doi:10.3390/md11062069

Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals

Laboratory of Toxinology, Department of Physiological Sciences, University of Brasília, Brasília, DF, 70910-900, Brazil
Author to whom correspondence should be addressed.
Received: 19 April 2013 / Revised: 28 May 2013 / Accepted: 30 May 2013 / Published: 14 June 2013
(This article belongs to the Special Issue Marine Peptides and Their Mimetics)
View Full-Text   |   Download PDF [1798 KB, uploaded 24 February 2015]   |  


The Kunitz-type protease inhibitors are the best-characterized family of serine protease inhibitors, probably due to their abundance in several organisms. These inhibitors consist of a chain of ~60 amino acid residues stabilized by three disulfide bridges, and was first observed in the bovine pancreatic trypsin inhibitor (BPTI)-like protease inhibitors, which strongly inhibit trypsin and chymotrypsin. In this review we present the protease inhibitors (PIs) described to date from marine venomous animals, such as from sea anemone extracts and Conus venom, as well as their counterparts in terrestrial venomous animals, such as snakes, scorpions, spiders, Anurans, and Hymenopterans. More emphasis was given to the Kunitz-type inhibitors, once they are found in all these organisms. Their biological sources, specificity against different proteases, and other molecular blanks (being also K+ channel blockers) are presented, followed by their molecular diversity. Whereas sea anemone, snakes and other venomous animals present mainly Kunitz-type inhibitors, PIs from Anurans present the major variety in structure length and number of Cys residues, with at least six distinguishable classes. A representative alignment of PIs from these venomous animals shows that, despite eventual differences in Cys assignment, the key-residues for the protease inhibitory activity in all of them occupy similar positions in primary sequence. The key-residues for the K+ channel blocking activity was also compared. View Full-Text
Keywords: protease inhibitor; Kunitz-type; serine protease; toxin; trypsin; chymotrypsin; venom protease inhibitor; Kunitz-type; serine protease; toxin; trypsin; chymotrypsin; venom

Figure 1

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Mourão, C.B.F.; Schwartz, E.F. Protease Inhibitors from Marine Venomous Animals and Their Counterparts in Terrestrial Venomous Animals. Mar. Drugs 2013, 11, 2069-2112.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top