Alamethicin

Alamethicin Structure
Alamethicin structure
Common Name Alamethicin
CAS Number 27061-78-5 Molecular Weight 1964.31000
Density N/A Boiling Point N/A
Molecular Formula C92H150N22O25 Melting Point 255-270ºC
MSDS Chinese USA Flash Point 188.6 °F
Symbol GHS06
GHS06
Signal Word Danger

The antimicrobial peptide gramicidin S permeabilizes phospholipid bilayer membranes without forming discrete ion channels.

Biochim. Biophys. Acta 1778(12) , 2814-22, (2008)

We examined the permeabilization of lipid bilayers by the beta-sheet, cyclic antimicrobial decapeptide gramicidin S (GS) in phospholipid bilayers formed either by mixtures of zwitterionic diphytanoylphosphatidylcholine and anionic diphytanoylphosphatidylglyce...

Interaction of the antibiotic minocycline with liver mitochondria - role of membrane permeabilization in the impairment of respiration.

FEBS J. 280(24) , 6589-99, (2013)

Several studies have proposed that the antibiotic minocycline (MC) has cytoprotective activities. Nevertheless, when cells have been exposed to MC at micromolar concentrations, detrimental effects have been also observed. Despite the known inhibitory activity...

ATP serves as an endogenous inhibitor of UDP-glucuronosyltransferase (UGT): a new insight into the latency of UGT.

Drug Metab. Dispos. 40(11) , 2081-9, (2012)

We have suggested that adenine-related compounds are allosteric inhibitors of UGT in rat liver microsomes (RLM) treated with detergent. To clarify whether the same occurs with a pore-forming peptide, alamethicin, the effects of adenine-related compounds on 4-...

Regulation of callose synthase activity in situ in alamethicin-permeabilized Arabidopsis and tobacco suspension cells.

BMC Plant Biol. 9 , 27, (2009)

The cell wall component callose is mainly synthesized at certain developmental stages and after wounding or pathogen attack. Callose synthases are membrane-bound enzymes that have been relatively well characterized in vitro using isolated membrane fractions o...

High Ca2+ load promotes hydrogen peroxide generation via activation of α-glycerophosphate dehydrogenase in brain mitochondria.

Free Radic. Biol. Med. 53(11) , 2119-30, (2012)

H(2)O(2) generation associated with α-glycerophosphate (α-GP) oxidation was addressed in guinea pig brain mitochondria challenged with high Ca(2+) load (10 μM). Exposure to 10 μM Ca(2+) induced an abrupt 2.5-fold increase in H(2)O(2) release compared to that ...

The lipid dependence of antimicrobial peptide activity is an unreliable experimental test for different pore models.

Biochemistry 51(51) , 10124-6, (2012)

Antimicrobial peptides usually kill bacteria by making their membranes permeable. Two main models (barrel-stave and Shai-Matsuzaki-Huang) have been proposed to describe the peptide-induced pores. Although several experimental tests can be exploited to discrim...

Inclusion of lateral pressure/curvature stress effects in implicit membrane models.

Biophys. J. 104(3) , 643-54, (2013)

Implicit membrane models usually treat the membrane as a hydrophobic slab and neglect lateral pressure/curvature stress effects. As a result, they cannot distinguish, for example, PE from PC lipids. Here, the implicit membrane model IMM1 is extended to includ...

Peptide-induced bilayer thinning structure of unilamellar vesicles and the related binding behavior as revealed by X-ray scattering.

Biochim. Biophys. Acta 1828(2) , 528-34, (2013)

We have studied the bilayer thinning structure of unilamellar vesicles (ULV) of a phospholipid 1,2-dierucoyl-sn-glycero-3-phosphocholine (di22:1PC) upon binding of melittin, a water-soluble amphipathic peptide. Successive thinning of the ULV bilayers with inc...

A thermodynamic approach to alamethicin pore formation.

Biochim. Biophys. Acta 1838(1 Pt B) , 98-105, (2014)

The structure and energetics of alamethicin Rf30 monomer to nonamer in cylindrical pores of 5 to 11Å radius are investigated using molecular dynamics simulations in an implicit membrane model that includes the free energy cost of acyl chain hydrophobic area e...

Alamethicin in bicelles: orientation, aggregation, and bilayer modification as a function of peptide concentration.

Biochim. Biophys. Acta 1828(11) , 2620-7, (2013)

Alamethicin is a 19-amino-acid residue hydrophobic peptide of the peptaibol family that has been the object of numerous studies for its ability to produce voltage-dependent ion channels in membranes. In this work, for the first time electron paramagnetic reso...