Bradykinin-potentiating peptides from the venom ofAgkistrodon halys blomhqffii

Zusammenfassung Aus dem Gift vonAgkistrodon halys blomhoffii konnten durch Säulenchromatographie an Sephadex G-100, G-25 und CM-Sephadex C-50 fünf Peptidkomponenten isoliert werden, welche die kontrahierende Wirkung von Bradykinin auf den isolierten Meerschweinchendarm signifikant erhöhen.

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Part of this paper was presented at the 41st Annual Meeting of the Japanese Biochemical Society, Tokyo (1968).     

Structure of potentiator A,one of the five bradykinin potentiating peptides from the venom ofAgkistrodon halys blomhoffii

Zusammenfassung Strukturaufklärung eines Bradykinnin-potenzierenden Peptids, Peptids A, aus dem Gift vonAgkistrodon halys blomhoffii.     

Structure of bradykinin-potentiating peptide containing tryptophan from the venom ofAgkistrodon halys blomhoffii

Zusammenfassung Es wird über die Strukturaufklärung eines Bradykinin-potenzierenden Peptids aus dem Gift vonAgkistrodon halys blomhoffii berichtet.     

A new pyroglutamylpeptide (Pyr-Lys-Ser) isolated from the venom ofAgkistrodon halys blomhoffii

Zusammenfassung Es wird über die Strukturklärung eines neuen pyroglutaminsäurehaltigen Peptids aus dem Gift vonAgkistrodon halys blomhoffii berichtet.     

Optical rotatory dispersion of proline-rich peptides from the venom ofBothrops jararaca

Zusammenfassung Die optische Rotationsdispersion mehrer prolinreicher Oligopeptide aus dem Gift der SchlangeBothrops jararaca wurde gemessen und mit jener von Oligoprolinen verglichen. Es konnte nur eine qualitative Beziehung zwischen der angedeuteten Strukturrigidität und der biologischen Wirksamkeit der Peptide festgestellt werden.

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This study was supported by a U.S. Public Health Service Grant No. 1RO1-AM-12473. ProfessorRosalia B. Frydman, Department of Biochemistry, University of Buenos Aires, Argentina, during her visit at Case Western Reserve University, participated in the experiments here reported.     

The insecticidal potential of venom peptides

Pest insect species are a burden to humans as they destroy crops and serve as vectors for a wide range of diseases including malaria and dengue. Chemical insecticides are currently the dominant approach for combating these pests. However, the de-registration of key classes of chemical insecticides due to their perceived ecological and human health risks in combination with the development of insecticide resistance in many pest insect populations has created an urgent need for improved methods of insect pest control. The venoms of arthropod predators such as spiders and scorpions are a promising source of novel insecticidal peptides that often have different modes of action to extant chemical insecticides. These peptides have been optimized via a prey–predator arms race spanning hundreds of millions of years to target specific types of insect ion channels and receptors. Here we review the current literature on insecticidal venom peptides, with a particular focus on their structural and pharmacological diversity, and discuss their potential for deployment as insecticides.     

Inhibition of angiotensin-converting enzyme by analogs of peptides fromBothrops jararaca venom

Zusammenfassung Nachweis mit Analogen der im Gifte vonBothrops jararaca gefundenen Peptide, dass die Inhihibition des Angiotensins «converting enzyme» von zwei eindeutigen Teilsequenzen dieser Peptide abhängig ist. Die hohe spezifische kompetitive Inhibition, hervorgerufen durch die Peptide vonBothrops jararaca, wird der Bindung ihrer Tripeptidreste vom Carboxyterminus mit dem aktiven Zentrum des Enzyms zugeschrieben, die in gleicher Weise wie die Peptidsubstrate mit dem Enzym gebunden werden. Die Wirksamkeit der Giftpeptide hängt von der Bindung eines zweiten Teiles der Peptide mit dem Enzym ab.     

Snake venom thrombin-like enzymes: from reptilase to now

The snake venom thrombin-like enzymes (SVTLEs) comprise a number of serine proteases functionally and structurally related to thrombin. Until recently, only nine complete sequences of this subgroup of the serine protease family were known. Over the past 5 years, the primary structure of several SVTLEs has been characterized, and now this family includes several members. Of particular interest is their possible use in pathologies such as thrombosis. The aim of the present review is to summarize the state of the art concerning the evolutionary, structural and biological features of the SVTLEs.Received 16 August 2003; received after revision 26 September 2003; accepted 1 October 2003     

Rate of structural renaturation of curare-like polypeptide from cobra venom]

After breakage of their four disulfide bonds, snake curare-like toxins recover spontaneously their native conformation at different rates depending on the number of residues in the sequence.