Melittin, a peptide from bee venom, is known to undergo a monomer / tetramer conversion in aqueous solutions. We have studied the possible participation of dimers in the association equilibrium of melittin by sedimentation equilibrium experiments in the analytical ultracentrifuge and subsequent mathematical analysis of the concentration distributions obtained. It was found that the dimeric state is not significantly populated, the contribution of dimer to the total peptide weight probably being below 0.5%.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1329324PMC
http://dx.doi.org/10.1016/S0006-3495(85)83786-3DOI Listing

Publication Analysis

Top Keywords

dimeric melittin
4
melittin occur
4
occur aqueous
4
aqueous solutions?
4
solutions? melittin
4
melittin peptide
4
peptide bee
4
bee venom
4
venom undergo
4
undergo monomer
4

Similar Publications

Dimerization and lysine substitution of melittin have differing effects on bacteria.

Front Pharmacol

October 2024

ACTV Research Group, Melbourne Dental School, Division of Basic and Clinical Oral Sciences, Royal Dental Hospital and The Bio21 Institute of Molecular Science and Biotechnology, The University of Melbourne, Melbourne, VIC, Australia.

Introduction: Melittin is a potent antimicrobial peptide from bee venom that is effective against both Gram-positive and Gram-negative bacteria. However, it is extremely toxic to mammalian cells and, as yet, has no clinical use. Modifications to its amino acid sequence, cyclization, truncation, and dimerization have been attempted in order to reduce its toxicity whilst maintaining its antimicrobial activity.

View Article and Find Full Text PDF

Unlabelled: The study aimed to investigate the antibacterial activity, cytotoxicity, and mechanism of action of the non-ionic, cyclic lipopeptide, serrawettin W2-FL10 against . W2-FL10 exhibited potent activity against the Gram-positive bacteria , , , and , with minimum inhibitory concentration (MIC) values ranging from 6.3 to 31.

View Article and Find Full Text PDF

From Milliseconds to Minutes: Melittin Self-Assembly from Concerted Non-Equilibrium Pressure-Jump and Equilibrium Relaxation Nuclear Magnetic Resonance.

J Phys Chem Lett

February 2024

Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 5 Memorial Drive, Bethesda, Maryland 20892, United States.

Non-equilibrium kinetics techniques like pressure-jump nuclear magnetic resonance (NMR) are powerful in tracking changes in oligomeric populations and are not limited by relaxation rates for the time scales of exchange that can be probed. However, these techniques are less sensitive to minor, transient populations than are Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments. We integrated non-equilibrium pressure-jump and equilibrium CPMG relaxation dispersion data to fully map the kinetic landscape of melittin tetramerization.

View Article and Find Full Text PDF

Cationic membrane-active toxins are the most abundant group of proteins in the venom of snakes and insects. Cationic proteins such as cobra venom cytotoxin and bee venom melittin are known for their pharmacological reactions including anticancer and antimicrobial effects which arise from the toxin-induced alteration in the dynamics and structure of plasma membranes and membranes of organelles. It has been established that these cationic toxins trigger the formation of non-bilayer lipid phase transitions in artificial and native mitochondrial membranes.

View Article and Find Full Text PDF

In this study, a chalcone-branched polyimide (CB-PI) was synthesized by the Steglich esterification reaction for selective recognition of the toxic peptide melittin (MEL). MEL was immobilized on a nanopatterned poly(dimethylsiloxane) (PDMS) mold using a conventional surface modification technique to increase binding sites. A stripe-nanopatterned thin CB-PI film was formed on a quartz crystal (QC) substrate by simultaneously performing microcontact printing and ultraviolet (UV) light dimerization using a MEL-immobilized mold.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!