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      Three Valuable Peptides from Bee and Wasp Venoms for Therapeutic and Biotechnological Use: Melittin, Apamin and Mastoparan

      review-article
      Author(s): * , *
      Editor(s):
      Publication date (Electronic):
      Journal: Toxins
      Publisher: MDPI
      Keywords: bee, wasp, venom, melittin, apamin, mastoparan

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          Abstract

          While knowledge of the composition and mode of action of bee and wasp venoms dates back 50 years, the therapeutic value of these toxins remains relatively unexploded. The properties of these venoms are now being studied with the aim to design and develop new therapeutic drugs. Far from evaluating the extensive number of monographs, journals and books related to bee and wasp venoms and the therapeutic effect of these toxins in numerous diseases, the following review focuses on the three most characterized peptides, namely melittin, apamin, and mastoparan. Here, we update information related to these compounds from the perspective of applied science and discuss their potential therapeutic and biotechnological applications in biomedicine.

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          Most cited references162

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          Endosomal escape pathways for delivery of biologicals.

          Amir K Varkouhi, Marije Scholte, Gert Storm … (2011)
          Despite continuous improvements in delivery systems, the development of methods for efficient and specific delivery of targeted therapeutic agents still remains an issue in biological treatments such as protein and gene therapy. The endocytic pathway is the major uptake mechanism of cells and any biological agents, such as DNA, siRNA and proteins. These agents become entrapped in endosomes and are degraded by specific enzymes in the lysosome. Thus, a limiting step in achieving an effective biological based therapy is to facilitate the endosomal escape and ensure cytosolic delivery of the therapeutics. Bacteria and viruses are pathogens which use different mechanisms to penetrate the membranes of their target cells and escape the endosomal pathway. Different mechanisms such as pore formation in the endosomal membrane, pH-buffering effect of protonable groups and fusion into the lipid bilayer of endosomes have been proposed to facilitate the endosomal escape. Several viral and bacterial proteins have been identified that are involved in this process. In addition, chemical agents and photochemical methods to rupture the endosomal membrane have been described. New synthetic biomimetic peptides and polymers with high efficacy in facilitating the endosomal escape, low pathogenicity and toxicity have been developed. Each strategy has different characteristics and challenges for designing the best agents and techniques to facilitate the endosomal escape are ongoing. In this review, several mechanisms and agents which are involved in endosomal escape are introduced. Copyright © 2010 Elsevier B.V. All rights reserved.
          Article 0 comments Cited 385 times – based on 0 reviews     Review now
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            Small-conductance Ca2+-activated K+ channels: form and function.

            John Adelman, James Maylie, Pankaj Sah (2012)
            Small-conductance Ca(2+)-activated K(+) channels (SK channels) are widely expressed throughout the central nervous system. These channels are activated solely by increases in intracellular Ca(2+). SK channels are stable macromolecular complexes of the ion pore-forming subunits with calmodulin, which serves as the intrinsic Ca(2+) gating subunit, as well as with protein kinase CK2 and protein phosphatase 2A, which modulate Ca(2+) sensitivity. Well-known for their roles in regulating somatic excitability in central neurons, SK channels are also expressed in the postsynaptic membrane of glutamatergic synapses, where their activation and regulated trafficking modulate synaptic transmission and the induction and expression of synaptic plasticity, thereby affecting learning and memory. In this review we discuss the molecular and functional properties of SK channels and their physiological roles in central neurons.
            Article 0 comments Cited 154 times – based on 0 reviews     Review now
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              Melittin: a membrane-active peptide with diverse functions.

              Amitabha Chattopadhyay, H Raghuraman (2007)
              Melittin is the principal toxic component in the venom of the European honey bee Apis mellifera and is a cationic, hemolytic peptide. It is a small linear peptide composed of 26 amino acid residues in which the amino-terminal region is predominantly hydrophobic whereas the carboxy-terminal region is hydrophilic due to the presence of a stretch of positively charged amino acids. This amphiphilic property of melittin has resulted in melittin being used as a suitable model peptide for monitoring lipid-protein interactions in membranes. In this review, the solution and membrane properties of melittin are highlighted, with an emphasis on melittin-membrane interaction using biophysical approaches. The recent applications of melittin in various cellular processes are discussed.
              Article 0 comments Cited 151 times – based on 0 reviews     Review now
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                Author and article information

                Contributors
                Sokcheon Pak: Role: Academic Editor
                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (iso-abbrev): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 01 April 2015
                Publication date Collection: April 2015
                Volume: 7
                Issue: 4
                Pages: 1126-1150
                Affiliations
                Chemistry and Molecular Pharmacology, Institute for Research in Biomedicine (IRB Barcelona), Baldiri i Reixac, 10, Barcelona 08028, Spain
                Author notes
                [* ]Authors to whom correspondence should be addressed; E-Mails: miguel.irbbarcelona@ 123456gmail.com (M.M.); ernest.giralt@ 123456irbbarcelona.org (E.G.); Tel.: +65-8191-9601 (M.M.); +34-9340-37126 (E.G.).
                Article
                Publisher ID: toxins-07-01126
                DOI: 10.3390/toxins7041126
                PMC ID: 4417959
                PubMed ID: 25835385
                SO-VID: 284c54d7-d072-4837-af64-670e0c4a1195
                Copyright © © 2015 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 04 February 2015
                Date accepted : 25 March 2015
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular medicine
                Keywords: bee,wasp,venom,melittin,apamin,mastoparan
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: bee, wasp, venom, melittin, apamin, mastoparan

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