Small peptides, big world: biotechnological potential in neglected bioactive peptides from arthropod venoms

Abstract

Until recently, a toxinologist's tasks involved the search for highly toxic or lethal toxins in animal venoms that could explain the harmful effects in clinically observed symptoms. Most of these toxins were put on evidence using a function to structure approach, in which a biological phenomena observation usually guided the isolation and characterization of the causative molecule. Paving this way, many toxins were promptly purified because of their readily observed effect. Nevertheless, small molecules with micro-effects that are not easily visualized can be relatively neglected or poorly studied. This situation has changed now with the advent of the sensitivity, resolution and accuracy of techniques such as mass spectrometry and proteomic approaches used in toxinology. Taking advantage of these methodologies, small peptides with 'newly exploited' biological activities such as vasoactive, hormone-like, antimicrobial and others have been recently given much more attention, enlarging the known repertoire of bioactive molecules found in animal venoms. This article aims to review current knowledge on small biologically active peptides (<3 kDa) found in arthropod venoms and discuss their potentialities as new drug candidates or therapeutic lead compounds.

Functional Hypervariability and Gene Diversity of Cardioactive Neuropeptides

“…The structural diversity of these regulatory peptidic scaffolds varies from small linear peptides such as enkephalins to more elaborate disulfide-constrained peptide hormones such as insulin. Related to these peptides, endogenous-like toxins are utilized exogenously by venomous animals as evident by their frequent discovery in venom (1). For example, sarafotoxins are potent mammalian vasoconstrictors found in snake venom (2), and are members of the endogenous hormone endothelin family (ϳ60% sequence homology).…”

Apitherapy Have a Role in Treatment of Multiple Sclerosis

“…The therapeutic benefits of honeybee venom have been known for a long time to relieve pain and to treat inflammatory diseases particularly for treatment of arthritic and rheumatic conditions in humans [21,22] and in animals [23][24][25]. Specific immunotherapy with bee venom can result in an almost complete protection against adverse (or allergic) reactions from stings in the great majority of cases [26].…”

Separating stereoisomers of di‐, tri‐, and tetrapeptides using capillary electrophoresis with contactless conductivity detection

“…Increasing the concentration of chiral crown ether from 5 to 10 mM further improved the resolutions for most of the peptides studied, but the resolution became poor for the peptides Gly -DL-Ala, and Gly -DLLeu -DL-Ala. On the other hand, as can be seen from Table 1. Migration times (t) and resolution (R s ) for the separation of the stereoisomers of peptides using a separation buffer consisting of 0.5 M acetic acid containing 5 mM DM-b-CD and 5 mM 18C 6 (3,4) the increase in Joule heating caused by the higher background conductivity. The degree of deprotonation of the chiral selector has an effect on the binding ability with peptides and it is therefore worthwhile to investigate the effect of the pH value of the buffer on separation.…”