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Introduction to electrical interfacial phenomena
Published in K.S. Birdi, Introduction to Electrical Interfacial Phenomena, 2010
As an example, the bee venom melittin is a very unique membrane protein (26-amino acid chain). It can penetrate into the BLM very easily because it is highly hydrophobic (very low solubility in water). However, the amino acid composition is unique, which induces a positive charge very near or at the cell interface. The proximity of this specific charge disrupts the BLM. The model membrane experiments have shown how these membrane proteins behave in real systems (see Chapter 3). Experiments have shown that the most useful procedure is to use the monolayer method, which was used by Langmuir (who was awarded the Nobel Prize for using this model membrane method) (Birdi, 2009). Melittin has recently been found to exhibit therapeutic activity. It has been reported to show powerful anti-inflammatory properties (for example, against rheumatoid arthritis).
Antimicrobial activity of the recombinant peptide Melittin-Thanatin with three glycine to tryptophan mutations
Published in Preparative Biochemistry & Biotechnology, 2023
Yong Liu, Xiuping Zhang, Chunyan Meng, Shengyue Ji, Kangkang Guo
Melittin was the main active component of bee venom, accounting for 50% of the dry weight of bee venom, and was the main substance in bee venom.[15] Melittin could be antibacterial, antiviral, anti-inflammatory, anti-radiation, and anticancer effect.[16] Melittin is composed of 26 amino acids, and its primary structure was GIGAVLKVLTTLPALISWIKRKRQQ.[17] Melittin had a strong inhibitory effect on gram-positive and gram-negative bacteria, but it also had a strong hemolytic activity, which limited the clinical application of Melittin. Since Melittin had the properties of destroying bacterial membranes and killing cells, obtaining active Melittin from prokaryotic or eukaryotic expression systems, it needed to be expressed in the form of fusion proteins.[18,19]