Phepropeptin C Proteasome Inhibitor
Product#: FNK-16966
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Phepropeptin C Proteasome Inhibitor
Cat No.: FNK-16966
Size: 1mg
Specifications
Code No : 16966
CAS# : 396729-25-2
Molecular Formula : C38H60N6O6
Molecular Weight : 696.934
Source : Streptomyces sp. MK600-cF7
Appearance : Powder
Purity : > 98% (HPLC)
Long Term Storage : at - 20 °C
Solubility : Soluble in MeOH, DMSO, DMF
Insoluble in H2O
Application Notes
Phepropeptin C was isolated from cultured broth of Streptomyces sp. MK600-cF7 as an inhibitor of proteasome (IC50 value 12.5 μg/ml). It showed no inhibition toward proteasomal trypsin-like activityand α-chymotrypsin from bovine pancreas at 100 μg/ml.
Description
Phepropeptin C is a cyclic hexapeptide compound that functions as a proteasome inhibitor.It belongs to a family of four related compounds named phepropeptins A, B, C, and D, which were isolated for their ability to inhibit proteasomes, cellular structures that play a crucial role in regulating many cellular functions.
The structure of phepropeptins consists of six amino acid residues arranged in a cyclic configuration. While the exact structure of Phepropeptin C is not explicitly stated in the search results, we can infer that it shares similarities with Phepropeptin B, which has the structure cyclo(-L-Leu-D-Phe-L-Pro-L-Phe-D-Leu-L-Val-). The phepropeptins differ from each other in two of their constituent amino acids, while four amino acid moieties remain conserved across all four compounds.
Phepropeptins, including Phepropeptin C, demonstrate selective inhibition of the proteasomal chymotrypsin-like activity. Importantly, they do not inhibit alpha-chymotrypsin, indicating a specific action on proteasomes rather than a general protease inhibition.
Phepropeptin C is available commercially as a research tool for studying proteasome inhibition. It has a CAS number of 396729-25-2 and is typically supplied with high purity (>98%).
References
1) Isolation and structural determination of pheptopeptins A, B, C and D, new proteasome inhibitors produced by
Streptomyces sp. Sekizawa R, et al. J Antibiot. 2001 54(11) 874-881.
Phepropeptin C was isolated from cultured broth of Streptomyces sp. MK600-cF7 as an inhibitor of proteasome (IC50 value 12.5 μg/ml). It showed no inhibition toward proteasomal trypsin-like activityand α-chymotrypsin from bovine pancreas at 100 μg/ml.
Description
Phepropeptin C is a cyclic hexapeptide compound that functions as a proteasome inhibitor.It belongs to a family of four related compounds named phepropeptins A, B, C, and D, which were isolated for their ability to inhibit proteasomes, cellular structures that play a crucial role in regulating many cellular functions.
The structure of phepropeptins consists of six amino acid residues arranged in a cyclic configuration. While the exact structure of Phepropeptin C is not explicitly stated in the search results, we can infer that it shares similarities with Phepropeptin B, which has the structure cyclo(-L-Leu-D-Phe-L-Pro-L-Phe-D-Leu-L-Val-). The phepropeptins differ from each other in two of their constituent amino acids, while four amino acid moieties remain conserved across all four compounds.
Phepropeptins, including Phepropeptin C, demonstrate selective inhibition of the proteasomal chymotrypsin-like activity. Importantly, they do not inhibit alpha-chymotrypsin, indicating a specific action on proteasomes rather than a general protease inhibition.
Phepropeptin C is available commercially as a research tool for studying proteasome inhibition. It has a CAS number of 396729-25-2 and is typically supplied with high purity (>98%).
References
1) Isolation and structural determination of pheptopeptins A, B, C and D, new proteasome inhibitors produced by
Streptomyces sp. Sekizawa R, et al. J Antibiot. 2001 54(11) 874-881.
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| Infectious Disease Prevention | Compound Name | Product Code | Link | ||||
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Natural macrocyclic compounds from microorganisms:
| Structural classification | Compound Name | Chemical Structure | Property / Biological activity | Link | ||||
|---|---|---|---|---|---|---|---|---|
| Bacterial proteins/Inhibition of DNA synthesis | Aplasmomycin (Sodium Salt) |  |
Aplasmomycin A Inhibited the growth of gram-positive bacteria including mycobacteria and showed an antimalarial activity in mice infected with Plasmodium berghei. | |
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| Migrastatin |  |
Migrastatin inhibited metastasis of human esophageal cancer cells and anchorage-independent growth of human small cell lung carcinoma cells. | |
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| Macrolactams | Bisucaberin |  |
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| Cyclic peptides | Bottromycin A2 |  |
Bottromycin A2 showed growth inhibitory activity against gram-positive bacteria, MRSA (Methicillin-resistant Staphylococcus aureus), and VRE (Vancomycin-resistant Enterococci). | |
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| Iturin A-2 |  |
Iturin A-2 showed the control of damping-off of tomato (a seedling disease) and cytotoxicity to human breast cancer cell line BT-474. | |
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| Plipastatin A1 |  |
Plipastatin A1 inhibited phospholipase A2 and induced ISR (induced-systemic-resistance). | |
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| Phepropeptin A |  |
Phepropeptin A inhibited proteasomal chymotrypsin-like activity. | |
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| Phepropeptin B |  |
Phepropeptin B inhibited proteasomal chymotrypsin-like activity. | |
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| Phepropeptin C |  |
Phepropeptin C inhibited proteasomal chymotrypsin-like activity. | Current Link | |||||
| Phepropeptin D |  |
Phepropeptin D inhibited proteasomal chymotrypsin-like activity. | |
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| Cycloalkenes | Rubratoxin A |  |
Rubratoxin A inhibited protein phosphatase 2A (PP2A) in a competitive manner. | |
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