| Identification | Back Directory | [Name]
PROTEASOME INHIBITOR I | [CAS]
158442-41-2 | [Synonyms]
PSI
N-Cb
CS-1340
Z-IE(OTBU)AL-CHO
PROTEASOME INHIBITOR I
ProteasoMe Inhibitor 1
PROTEASOME INHIBITOR PSI
M.W. 618.77 C32H50N4O8
Z-ILE-GLU(OBUT)-ALA-LEU-H
Z-ILE-GLU(OTBU)-ALA-LEU-CHO
PSI PROTEASOME INHIBITOR I
Cbz-Ile-Glu(OtBu)-Ala-Leu-al
Z-ILE-GLU(OTBU)-ALA-LEUCINAL
Z-ILE-GLU(OTBU)-ALA-LEU-ALDEHYDE
PROTEASOME INHIBITOR I USP/EP/BP
z-ile-glu(o-t-butyl)-ala-leucinal
PROTEASOME INHIBITOR I (ALDEHYDE)
CBZ-Ile-Glu(OtBu)-Ala-Leu-aldehyde
Z-ILE-GLU(OBUT)-ALA-LEU-H (ALDEHYDE)
N-CBZ-ILE-GLU(O-T-BUTYL)-ALA-LEUCINAL
N-carbobenzyloxy-Ile-Glu(O-tert-butyl)-Ala-leucinal
PROTEASOME INHIBITOR I ;Z-ILE-GLU(OTBU)-ALA-LEU-CHO
arbobenzoxy-l-isoleucyl-gamma-t-butyl-l-glutamyl-l-alanyl-l-leucinal
CARBOBENZOXY-L-ISOLEUCYL-GAMMA-T-BUTYL-L-GLUTAMYL-L-ALANYL-L-LEUCINAL
BENZYLOXYCARBONYL-L-ISOLEUCYL-[(2S)-2-AMINO-4-(T-BUTYLOXYCARBONYL)BUTANOYL]-L-ALANYL-L-LEUCINAL
N-[(Phenylmethoxy)carbonyl]-L-isoleucyl-L-α-glutamyl-tert-butylester-N-[(1S)-1-formyl-3-methylbutyl]-L-alaninamide
L-Alaninamide, N-[(phenylmethoxy)carbonyl]-L-isoleucyl-L-α-glutamyl-N-[(1S)-1-formyl-3-methylbutyl]-, 1,1-dimethylethyl ester
L-AlaninaMide, N-[(phenylMethoxy)carbonyl]-L-isoleucyl-L-a-glutaMyl-N-[(1S)-1-forMyl-3 -Methylbutyl]-, 1,1-diMethylethyl ester | [Molecular Formula]
C32H50N4O8 | [MDL Number]
MFCD00671409 | [MOL File]
158442-41-2.mol | [Molecular Weight]
618.76 |
| Chemical Properties | Back Directory | [Boiling point ]
844.2±65.0 °C(Predicted) | [density ]
1.121±0.06 g/cm3(Predicted) | [storage temp. ]
−20°C | [solubility ]
≥30.6 mg/mL in DMSO; insoluble in H2O; ≥48.7 mg/mL in EtOH | [form ]
solid | [pka]
11.12±0.46(Predicted) | [color ]
White to off-white |
| Hazard Information | Back Directory | [Uses]
Proteasome Inhibitor 1, is a drug that blocks the action of proteasomes, protein complexes that degrade unneeded and damaged proteins. It is also shown to be used for the treatment of cancer, especially multiple myeloma. Proteasome inhibitors also induce apoptosis and reduce viral replication in primary effusion lymphoma cells. | [Biological Activity]
zie(otbu)al-cho (psi)1 have been shown to inhibit the proteasome activities in a variety of cell types.peptide aldehyde, psi (z-ile-glu(otbu)-ala-leu-al), inhibits the proteasome 10-fold better than calpain but is less potent than mg1322. since mg132, psi, mg115 (z-leu-leu-nval-al) and alln can all inhibit calpains and various lysosomal cathepsins in addition to the proteasome, when using these inhibitors in cell culture it is important to perform control experiments to con￠rm that the observed e?ects are due to the inhibition of the proteasome. first, one can use agents, which block intracellular cysteine proteases, but do not inhibit proteasomes3. such inhibitors are z-leu-leu- al, and e-64 for calpains4, and weak bases such as chloroquine and e-64 for lysosomal proteolysis . in yeast, where digestive vacuoles contain mainly serine, not cysteine, proteases, phenylmethylsulfonyl ￡uoride can be used to inhibit these enzymes without affecting proteasomes5.despite the availability of these inhibitors, mg132, due to its low cost and the rapid reversibility of its action, still remains, in our opinion, the first choice to study proteasome involvement in a process in cell cultures or tissues, if appropriate controls are used. as the most potent and selective of commercially available aldehydes, mg132 is preferable to alln, mg115 (z-leu-leu-nval-al), or even psi. on the other hand, the least selective inhibitor, alln, because of its ability to inhibit most major pro teases in mammalian cells, is probably the best tool for prevention of unwanted proteolysis, for example during isolation of proteins from mammalian cells. | [References]
1. takada k (1995) mol. biol. rep. 21: 21–26 2. a. f. kisselev, a. l. goldberg. proteasome inhibitors: from research tools to drug candidates. chemistry & biology 8 (2001) 739-758. 3. w. matthews, j. driscoll, k. tanaka, a. ichihara, a.l. goldberg, involvement of the proteasome in various degradative processes in mammalian cells, proc. natl. acad. sci. usa 86 (1989) 2597-2601. 4. s. tsubuki, y. saito, m. tomioka, h. ito, s. kawashima, differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine, j. biochem. 119 (1996) 572-576. 5. d.h. lee, a.l. goldberg, selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in saccharomyces cerevisiae, j. biol. chem. 271 (1996) 27280-27284. |
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