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Mastoparan X

CAS# 72093-22-2

Mastoparan X

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Chemical structure

Mastoparan X

3D structure

Chemical Properties of Mastoparan X

Cas No. 72093-22-2 SDF Download SDF
PubChem ID 5488554 Appearance Powder
Formula C73H126N20O15S M.Wt 1555.98
Type of Compound N/A Storage Desiccate at -20°C
Solubility Soluble to 1 mg/ml in sterile water
Chemical Name (2S)-N-[(2S)-1-[[(2S)-6-amino-1-[[2-[[(3S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-6-amino-1-[[(2S)-6-amino-1-[[(2S)-1-[[(2S)-1-amino-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxohexan-2-yl]amino]-1-oxohexan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-1-oxohexan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]butanediamide
SMILES CCC(C)C(C(=O)NC(CC(=O)N)C(=O)NC(CC1=CNC2=CC=CC=C21)C(=O)NC(CCCCN)C(=O)NCC(=O)NC(C(C)CC)C(=O)NC(C)C(=O)NC(C)C(=O)NC(CCSC)C(=O)NC(C)C(=O)NC(CCCCN)C(=O)NC(CCCCN)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)N)N
Standard InChIKey FYJKBFOGJAVCAL-KCQOFHQJSA-N
Standard InChI InChI=1S/C73H126N20O15S/c1-13-41(7)59(78)72(107)92-56(36-57(77)94)71(106)91-55(35-46-37-80-48-24-16-15-23-47(46)48)70(105)87-49(25-17-20-29-74)65(100)81-38-58(95)93-60(42(8)14-2)73(108)84-43(9)62(97)82-44(10)63(98)86-52(28-32-109-12)66(101)83-45(11)64(99)85-50(26-18-21-30-75)67(102)88-51(27-19-22-31-76)68(103)90-54(34-40(5)6)69(104)89-53(61(79)96)33-39(3)4/h15-16,23-24,37,39-45,49-56,59-60,80H,13-14,17-22,25-36,38,74-76,78H2,1-12H3,(H2,77,94)(H2,79,96)(H,81,100)(H,82,97)(H,83,101)(H,84,108)(H,85,99)(H,86,98)(H,87,105)(H,88,102)(H,89,104)(H,90,103)(H,91,106)(H,92,107)(H,93,95)/t41-,42-,43-,44-,45-,49-,50-,51-,52-,53-,54-,55-,56-,59-,60?/m0/s1
General tips For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months.
We recommend that you prepare and use the solution on the same day. However, if the test schedule requires, the stock solutions can be prepared in advance, and the stock solution must be sealed and stored below -20℃. In general, the stock solution can be kept for several months.
Before use, we recommend that you leave the vial at room temperature for at least an hour before opening it.
About Packaging 1. The packaging of the product may be reversed during transportation, cause the high purity compounds to adhere to the neck or cap of the vial.Take the vail out of its packaging and shake gently until the compounds fall to the bottom of the vial.
2. For liquid products, please centrifuge at 500xg to gather the liquid to the bottom of the vial.
3. Try to avoid loss or contamination during the experiment.
Shipping Condition Packaging according to customer requirements(5mg, 10mg, 20mg and more). Ship via FedEx, DHL, UPS, EMS or other couriers with RT, or blue ice upon request.

Biological Activity of Mastoparan X

DescriptionAmphiphilic G protein activator peptide that binds to Gi and Go. Also binds with high affinity to calmodulin (Kd ~ 0.9 nM) and inhibits sarcoplasmic reticulum Ca2+-ATPase (Ki = 4.4 mM).

Mastoparan X Dilution Calculator

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Preparing Stock Solutions of Mastoparan X

1 mg 5 mg 10 mg 20 mg 25 mg
1 mM 0.6427 mL 3.2134 mL 6.4268 mL 12.8536 mL 16.067 mL
5 mM 0.1285 mL 0.6427 mL 1.2854 mL 2.5707 mL 3.2134 mL
10 mM 0.0643 mL 0.3213 mL 0.6427 mL 1.2854 mL 1.6067 mL
50 mM 0.0129 mL 0.0643 mL 0.1285 mL 0.2571 mL 0.3213 mL
100 mM 0.0064 mL 0.0321 mL 0.0643 mL 0.1285 mL 0.1607 mL
* Note: If you are in the process of experiment, it's necessary to make the dilution ratios of the samples. The dilution data above is only for reference. Normally, it's can get a better solubility within lower of Concentrations.

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References on Mastoparan X

Characterization of the structure and dynamics of mastoparan-X during folding in aqueous TFE by CD and NMR spectroscopy.[Pubmed:18008325]

Biopolymers. 2008 Mar;89(3):197-209.

Mastoparan-X, a 14-residue peptide found in wasp venom, does not adopt a well-defined structure in water, but it folds into an alpha-helix upon addition of trifluoroethanol (TFE). At low levels of TFE, the peptide is partially folded, passing through intermediate stages of folding as the amount of TFE is increased. These partially folded states have been characterized by CD and NMR spectroscopy, and methods to estimate the helical content from CD, chemical shift, and nuclear overhauser effect (NOE) data are compared. Variation in the sign and intensity of NOE cross-peaks is observed in different regions of the peptide, indicative of greater mobility of the sidechains compared to the backbone of the peptide. Furthermore, variation in the sidechain mobility is observed, both between sidechains of different amino acids and within the sidechain of a given amino acid. By monitoring chemical shifts and NOE intensities as the TFE concentration is increased, the initiation site for helix formation could be identified. Furthermore, details of the peptide structure and dynamics during the folding process were elucidated.

Selective acylation enhances membrane charge sensitivity of the antimicrobial peptide mastoparan-x.[Pubmed:21244836]

Biophys J. 2011 Jan 19;100(2):399-409.

The partitioning of the wasp venom peptide mastoparan-X (MPX) into neutral and negatively charged lipid membranes has been compared with two new synthetic analogs of MPX where the N(alpha)-terminal of MPX was acylated with propanoic acid (PA) and octanoic acid (OA). The acylation caused a considerable change in the membrane partitioning properties of MPX and it was found that the shorter acylation with PA gave improved affinity and selectivity toward negatively charged membranes, whereas OA decreased the selectivity. Based on these findings, we hypothesize that minor differences in the embedding and positioning of the peptide in the membrane caused by either PA or OA acylation play a critical role in the fine-tuning of the effective charge of the peptide and thereby the fine-tuning of the peptide's selectivity between neutral and negatively charged lipid membranes. This finding is unique compared to previous reports where peptide acylation enhanced membrane affinity but also resulted in impaired selectivity. Our result may provide a method of enhancing selectivity of antimicrobial peptides toward bacterial membranes due to their high negative charge-a finding that should be investigated for other, more potent antimicrobial peptides in future studies.

Side chain hydrophobicity modulates therapeutic activity and membrane selectivity of antimicrobial peptide mastoparan-X.[Pubmed:24621994]

PLoS One. 2014 Mar 12;9(3):e91007.

The discovery of new anti-infective compounds is stagnating and multi-resistant bacteria continue to emerge, threatening to end the "antibiotic era". Antimicrobial peptides (AMPs) and lipo-peptides such as daptomycin offer themselves as a new potential class of antibiotics; however, further optimization is needed if AMPs are to find broad use as antibiotics. In the present work, eight analogues of mastoparan-X (MPX) were investigated, having side chain modifications in position 1, 8 and 14 to modulate peptide hydrophobicity. The self-association properties of the peptides were characterized, and the peptide-membrane interactions in model membranes were compared with the bactericidal and haemolytic properties. Alanine substitution at position 1 and 14 resulted in higher target selectivity (red blood cells versus bacteria), but also decreased bactericidal potency. For these analogues, the gain in target selectivity correlated to biophysical parameters showing an increased effective charge and reduction in the partitioning coefficient for membrane insertion. Introduction of an unnatural amino acid, with an octyl side chain by amino acid substitution, at positions 1, 8 and 14 resulted in increased bactericidal potency at the expense of radically reduced membrane target selectivity. Overall, optimized membrane selectivity or bactericidal potency was achieved by changes in side chain hydrophobicity of MPX. However, enhanced potency was achieved at the expense of selectivity and vice versa in all cases.

Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.[Pubmed:27513014]

J Phys Chem Lett. 2016 Sep 1;7(17):3365-70.

The mechanism of protein insertion into a lipid bilayer is poorly understood because the kinetics of this process is difficult to measure. We developed a new approach to study insertion of the antimicrobial peptide Mastoparan X into zwitterionic lipid vesicles, using a laser-induced temperature-jump to initiate insertion on the microsecond time scale and infrared and fluorescence spectroscopies to follow the kinetics. Infrared probes the desolvation of the peptide backbone and yields biphasic kinetics with relaxation lifetimes of 12 and 117 mus, whereas fluorescence probes the intrinsic tryptophan residue located near the N-terminus and yields a single exponential phase with a lifetime of 440 mus. Arrhenius analysis of the temperature-dependent rates yields an activation energy for insertion of 96 kJ/mol. These results demonstrate the complexity of the insertion process and provide mechanistic insight into the interplay between peptides and the lipid bilayer required for peptide transport across cellular membranes.

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