Product Name

MELITTIN

Description

Natural, non-synthetic, polypeptide from European honey bee, Apis mellifera, venom; the principle hemolytic component

Amino Acid Sequence

{GLY}{ILE}{GLY}{ALA}{VAL}{LEU}{LYS}{VAL}{LEU}{THR}
{THR}{GLY}{LEU}{PRO}{ALA}{LEU}{ILE}{SER}{TRP}{ILE}
{LYS}{ARG}{LYS}{ARG}{GLN}{GLN}-NH2

IDNUMBER/Order Ref.

Melittin, CAS 20449-79-0

CAS Registry Number

20449-79-0

MDL Number

MFCD00076868

Molecular Formula

C131 H229 N39 O31

Molecular Weight

2846.46

APPEARANCE

Dry fluffy powder, pale-yellow color

Original Storage Container

Storage temperature

-20°C

Transportation (short-term) temperature

Ambient

SOLUBILITY

Solubility in an aqueous medium; melittin is soluble as a tetramer in aqueous salt solutions.

PURITY (HPLC)

>97%

Known Activity

26-residue polypeptide binds calmodulin in a Ca2+ dependent manner, activates phospholipase A2,

inhibits protein kinase C (IC50 = 5 – 7 mM) by binding to the catalytic domain in a Mg-ATP sensitive manner.

Highly sensitive substrate for chymotrypsin detection.

Please refer to below references and selected article abstracts on extensive application of Melittin.

References

Baudier, J., et al. Biochemistry 26, 2886, (1987)

Bechinger, B. Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin.

J. of Membrane Biology. Vol.156, Num3/April, 1997.

Boman, H.G. et al. Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. Dept of Microbiology, University of Stockholm, Sweden. FEBS Lett. 1989 Dec 18;259(1):103-6.

Comte, M. et al. Ca2+-dependent high-affinity complex formation between calmodulin and melittin.Biochem J. 1983 January 1; 209(1): 269–272.

Cuppoletti, J., and Abbott, A.J. Arch. Biochem. Biophys. 283, 249, (1990)

DeGrado, W.F. et al. Kinetics and mechanism of hemolysis induced by melittin and by a synthetic melittin analogue. Biophys J. 1982 January; 37(1): 329–338.

Ghosh, A. K. et al. Modulation of Tryptophan Environment in Membrane-Bound Melittin by Negatively Charged Phospholipids: Implications in Membrane Organization and Function. Biochemistry, 36 (47), 14291 -14305, 1997. bi971933j S0006-2960(97)01933-8

Hristova K, et al. Structure, location, and lipid perturbations of melittin at the membrane interface. Biochim Biophys Acta. 1990 May 7;1031(2):143-61.

Jarrett, H.W., and Madhavan, R. J. Biol. Chem. 266, 362, (1991)

Lauterwein, J. et al. Physicochemical studies of the protein-lipid interactions in melittin-containing micelles. Biochim Biophys Acta. 1979 Sep 21;556(2):244-64.

Loutet SA, et al. A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo. J Bacteriol. Mar 2006;188(6):2073-2080.

Saugar JM, et al. Activity of cecropin A-melittin hybrid peptides against colistin-resistant clinical strains of Acinetobacter baumannii: molecular basis for the differential mechanisms of action. Antimicrob Agents Chemother. Apr 2006;50(4):1251-1256.

Shank LP, et al. Redesigning channel-forming peptides: amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity. Biophys J. Mar 15 2006;90(6):2138-2150

Terwilliger, TC., Eisenberg, D. The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem., Vol. 257, Issue 11, 6010-6015, 06, 1982

Tosteson, M.T., Tosteson D.C. The sting. Melittin forms channels in lipid bilayers. Biophysical Journal 36: 109-116 (1981) © 1981 the Biophysical Society.