A novel peptide from Apis mellifera and solid-phase synthesis of its analogue

Meng, Yu; Yang, Xiao Xiao; Sheng, Yu Xin; Zhang, Jin Lan; Yu, De Quan

doi:10.1016/j.cclet.2012.09.003

Cited by 12 publications

(5 citation statements)

References 13 publications

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“…Secapin is composed of 25 aa residues with a weight of 2866.5 Da. Its sequence of aa is YIIDVPPRCPPGSKFIKNRCRVIVP with a disulfide bridge in its structure that connects aa 9 with 20 [90,91]. Secapin represents around the 1% of BV composition, although it has been studied that this proportion increases in the case of queen-bee venom glands.…”

Section: Minor Peptidesmentioning

confidence: 99%

Bee Venom: An Updating Review of Its Bioactive Molecules and Its Health Applications

2020

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Bee venom (BV) is usually associated with pain since, when humans are stung by bees, local inflammation and even an allergic reaction can be produced. BV has been traditionally used in ancient medicine and in acupuncture. It consists of a mixture of substances, principally of proteins and peptides, including enzymes as well as other types of molecules in a very low concentration. Melittin and phospholipase A2 (PLA2) are the most abundant and studied compounds of BV. Literature of the main biological activities exerted by BV shows that most studies focuses on the comprehension and test of anti-inflammatory effects and its mechanisms of action. Other properties such as antioxidant, antimicrobial, neuroprotective or antitumor effects have also been assessed, both in vitro and in vivo. Moreover, human trials are necessary to confirm those clinical applications. However, notwithstanding the therapeutic potential of BV, there are certain problems regarding its safety and the possible appearance of adverse effects. On this perspective, new approaches have been developed to avoid these complications. This manuscript is aimed at reviewing the actual knowledge on BV components and its associated biological activities as well as the latest advances on this subject.

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Section: Minor Peptidesmentioning

confidence: 99%

Bee Venom: An Updating Review of Its Bioactive Molecules and Its Health Applications

2020

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“…The peptides Scapin, Scapin-1, and Scapin-2 are all 25 amino acid residues in length and share a similar secondary structure, with a disulfide bridge between Cys 9 and Cys 20. These peptides have been isolated from the venom of various species, such as Scapin from European Apis mellifera [ 16 ], Scapin-1 from Chinese Apis mellifera [ 17 ], and Scapin-2 from the Africanized honeybee. These compounds induce leukotriene-mediated hyperalgesia and edema [ 18 ].…”

Section: Introductionmentioning

confidence: 99%

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

Moreno

Giralt

2015

Toxins

297

261

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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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“…A hybrid undecapeptide derived from the well-known cecropin A and melittin showed antifungal and antibacterial activities. It also displays low cytotoxicity [84] similar to retro and retro-enantio analogs [85]. It also acts as an antibiotic and anti-malarial agent [86].…”

Section: Antimicrobial Activitymentioning

confidence: 98%

Hymenoptera Toxins: Biological Activity, Pharmaceutical and Therapeutic Uses

Sharma

Upadhyay

2021

Int J Pharm Pharm Sci

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The present review article explains the salient features of hornet venom toxins, their physiological, biological and pharmacological effect on animals and man. Hornets sting very fast and inflict venom, which is more dangerous than those of bees. Hornet venom contains both proteinaceous and non-proteinaceous peptides i.e. scapin, adolapin, mellitin, mastoparans and enzymes, mainly phospholipase and hyaluronidase, which show multiple biological effects i.e. cytolytic, hemotoxic, neuro-inhibitor, anticancer, anti-parasitic, immune hypersensitive, inflammatory, antimicrobial and anti-insect activities. Hornet stings are more painful to humans than typical wasp stings because hornet venom contains a large amount (5%) of acetylcholine. Hornet toxin components interact with receptors, ion channels and gated channels and affect the permeability functions of cells. Heavy envenomation shows quick pathophysiological lethal effects in man and pet. This article emphasizes the use of various hornet venom components for the production of disease-modifying anti-rheumatic and analgesic, anticancer drugs and insecticides. Hornet venom allergens could be used to prepare the rational design of component-resolved diagnosis of allergy and venom immunotherapy of inflicting patients.

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A novel peptide from Apis mellifera and solid-phase synthesis of its analogue

Cited by 12 publications

References 13 publications

Bee Venom: An Updating Review of Its Bioactive Molecules and Its Health Applications

Bee Venom: An Updating Review of Its Bioactive Molecules and Its Health Applications

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

Hymenoptera Toxins: Biological Activity, Pharmaceutical and Therapeutic Uses

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