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Toxins 2018, 10(11), 474;

Snake Venom Peptides: Tools of Biodiscovery

Department of Chemistry, University of Engineering and Technology, Lahore 54890, Pakistan
H.E. J. Research Institute of Chemistry, (ICCBS), University of Karachi, Karachi 75270, Pakistan
Botany Division, Institute of Pure and Applied Biology, Bahauddin Zakariya University, Multan 60800, Pakistan
Department of Chemistry, Institute of Biochemistry and Molecular Biology, University of Hamburg, 22607 Hamburg, Germany
Laboratory for Structural Biology of Infection and Inflammation, DESY, Build. 22a, Notkestr. 85, 22603 Hamburg, Germany
Authors to whom correspondence should be addressed.
Received: 14 October 2018 / Revised: 30 October 2018 / Accepted: 7 November 2018 / Published: 14 November 2018
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Nature endowed snakes with a lethal secretion known as venom, which has been fine-tuned over millions of years of evolution. Snakes utilize venom to subdue their prey and to survive in their natural habitat. Venom is known to be a very poisonous mixture, consisting of a variety of molecules, such as carbohydrates, nucleosides, amino acids, lipids, proteins and peptides. Proteins and peptides are the major constituents of the dry weight of snake venoms and are of main interest for scientific investigations as well as for various pharmacological applications. Snake venoms contain enzymatic and non-enzymatic proteins and peptides, which are grouped into different families based on their structure and function. Members of a single family display significant similarities in their primary, secondary and tertiary structures, but in many cases have distinct pharmacological functions and different bioactivities. The functional specificity of peptides belonging to the same family can be attributed to subtle variations in their amino acid sequences. Currently, complementary tools and techniques are utilized to isolate and characterize the peptides, and study their potential applications as molecular probes, and possible templates for drug discovery and design investigations. View Full-Text
Keywords: polypeptide structure and function; therapeutic peptides; X-ray crystallography; three-finger toxins; bradykinin potentiating peptides; crotamine; kunitz-type inhibitor polypeptide structure and function; therapeutic peptides; X-ray crystallography; three-finger toxins; bradykinin potentiating peptides; crotamine; kunitz-type inhibitor

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Munawar, A.; Ali, S.A.; Akrem, A.; Betzel, C. Snake Venom Peptides: Tools of Biodiscovery. Toxins 2018, 10, 474.

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