MDPI Contact

MDPI AG
St. Alban-Anlage 66,
4052 Basel, Switzerland
Support contact
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18

For more contact information, see here.

Advanced Search

You can use * to search for partial matches.

Search Results

1 article matched your search query. Search Parameters:
Authors = Sönke Harder

Matches by word:

SONKE (6) , HARDER (44)

View options
order results:
result details:
results per page:
Articles per page View Sort by
Displaying article 1-50 on page 1 of 1.
Export citation of selected articles as:
Open AccessArticle Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis
Toxins 2014, 6(3), 850-868; doi:10.3390/toxins6030850
Received: 3 November 2013 / Revised: 24 January 2014 / Accepted: 5 February 2014 / Published: 28 February 2014
Cited by 7 | Viewed by 2210 | PDF Full-text (1208 KB) | HTML Full-text | XML Full-text
Abstract
Elapid snake venom is a highly valuable, but till now mainly unexplored, source of pharmacologically important peptides. We analyzed the peptide fractions with molecular masses up to 10 kDa of two elapid snake venoms—that of the African cobra, N. m. mossambica (genus Naja
[...] Read more.
Elapid snake venom is a highly valuable, but till now mainly unexplored, source of pharmacologically important peptides. We analyzed the peptide fractions with molecular masses up to 10 kDa of two elapid snake venoms—that of the African cobra, N. m. mossambica (genus Naja), and the Peninsula tiger snake, N. scutatus, from Kangaroo Island (genus Notechis). A combination of chromatographic methods was used to isolate the peptides, which were characterized by combining complimentary mass spectrometric techniques. Comparative analysis of the peptide compositions of two venoms showed specificity at the genus level. Three-finger (3-F) cytotoxins, bradykinin-potentiating peptides (BPPs) and a bradykinin inhibitor were isolated from the Naja venom. 3-F neurotoxins, Kunitz/basic pancreatic trypsin inhibitor (BPTI)-type inhibitors and a natriuretic peptide were identified in the N. venom. The inhibiting activity of the peptides was confirmed in vitro with a selected array of proteases. Cytotoxin 1 (P01467) from the Naja venom might be involved in the disturbance of cellular processes by inhibiting the cell 20S-proteasome. A high degree of similarity between BPPs from elapid and viperid snake venoms was observed, suggesting that these molecules play a key role in snake venoms and also indicating that these peptides were recruited into the snake venom prior to the evolutionary divergence of the snakes. Full article
(This article belongs to the collection Evolution of Venom Systems)

Years

Subjects

Refine Subjects

Journals

Refine Journals

Article Types

Refine Types

Countries

Refine Countries
Back to Top