Our Group organises 3000+ Global Conferenceseries Events every year across USA, Europe & Asia with support from 1000 more scientific Societies and Publishes 700+ Open Access Journals which contains over 50000 eminent personalities, reputed scientists as editorial board members.

Open Access Journals gaining more Readers and Citations
700 Journals and 15,000,000 Readers Each Journal is getting 25,000+ Readers

This Readership is 10 times more when compared to other Subscription Journals (Source: Google Analytics)

Isolation and synthesis for secapin from bee venom (Apis mellifera L.)

Joint Event on 4th European Biopharma Congress & 6th International Conference and Exhibition on Pharmacology and Ethnopharmacology

Hesham R El-Seedi, Aida Abd El Wahed, Sunithi Gunasekera and Ulf Goransson

Uppsala University, Sweden Plant Protection Research Institute-Agricultural Research Centre, Egypt El-Menoufia University, Egypt

Posters & Accepted Abstracts: Clin Pharmacol Biopharm

DOI: 10.4172/2167-065X-C1-026

Abstract
Bee venom is highly rich in peptides and enzymes constituents, some of which are well-characterized functional agents such as melittin, apamin, and phospholipase A2 with potent bioactivities. Secapin in particular has attracted growing interest due to its role in the insect innate immune system as a hemolytic agent and due to its known applications in neurological, cardiovascular and immunological research areas. Secapin was first identified in early 1970s, but due its scarcity, detailed phytochemical investigations of secapin have been limited. Thus, it had also been challenging to introduce secapin to a wider range of medical and pharmaceutical applications. In the current work, we isolated secapin from bee venom (Apis mellifera), employing RP-HPLC and mass spectrometry. We successfully synthesized secapin for the first time using microwave-assisted Fmoc solid-phase peptide synthesis, followed by oxidative folding. The secondary structure was elucidated by a combination of techniques including MS, LC-MS, MS2, and 2D-NMR to characterize the pure native peptide.
Biography
Top