Detail of > 26305-03-3
- MSDS Download

- CAS Number:
- 26305-03-3
- Name:
L-Alaninamide,N-(3-methyl-1-oxobutyl)-L-valyl-L-valyl-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoyl-N-[(1S)-1-[(1S)-2-carboxy-1-hydroxyethyl]-3-methylbutyl]-
- Superlist Name:
- Pepstatin
- Formula:
- C34H63N5O9
- Molecular Structure:
![Molecular Structure of 26305-03-3 (L-Alaninamide,N-(3-methyl-1-oxobutyl)-L-valyl-L-valyl-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoyl-N-[(1S)-1-[(1S)-2-carboxy-1-hydroxyethyl]-3-methylbutyl]-)](http://www.lookchem.com/300w/2010/0620/26305-03-3.jpg)
- Synonyms:
- Pepstatin A: synthetic;L-Valinamide,N-(3-methyl-1-oxobutyl)-L-valyl-N-[4-[[2-[[1-(2-carboxy-1-hydroxyethyl)-3-methylbutyl]amino]-1-methyl-2-oxoethyl]amino]-2-hydroxy-1-(2-methylpropyl)-4-oxobutyl]-,[1S-[1R*,2R*,4[R*[R*(R*)]]]]-;Ahpatinin C;Heptanoic acid, N-(3-methyl-1-oxobutyl)-L-valyl-L-valyl-(3S,4S)-3-hydroxy-6-methyl-4-aminoheptanoyl-L-alanyl-(3S,4S)-3-hydroxy-6-methyl-4-amino-;Isovaleryl-L-valyl-L-valyl-4-amino-3-hydroxy-6-methylheptanoyl-L-alanyl-4-amino-3-hydroxy-6-methylheptanoicacid;N-(3-Methyl-1-oxobutyl)-L-valyl-L-valyl-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoyl-L-alanyl-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoicacid;N-Isovaleryl-L-valyl-L-valyl-3-hydroxy-6-methyl-g-aminoheptanoyl-L-alanyl-3-hydroxy-6-methyl-g-aminoheptanoic acid;NSC 272671;Pepsin inhibitor S 735A;Pepstatin;Pepstatin A;Procidin S 735A;
- Molecular Weight:
- 686.02
- EINECS:
- 247-600-0
- Density:
- 1.117 g/cm3
- Melting Point:
- 233 °C (dec.)(lit.)
- Boiling Point:
- 997.6 °C at 760 mmHg
- Flash Point:
- 557.1 °C
- Solubility:
- 10% acetic acid in methanol: 1 mg/mL
- Appearance:
- solid
- Safety:
- 22-24/25Details
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Reference
- Treatment of mouse muscular dystrophy with the protease inhibitor pepstatin
- Treatment of mouse muscular dystrophy with the protease inhibitor pepstatin. Schorr, Ewa E. Chelmicka; Arnason, Barry G. W.; Astrom, Karl-Eric; Darzynkiewicz, Zbigniew (Dep. Neurol., Univ. Chicago, Chicago, Ill., USA). J. Neuropathol. Exp. Neurol., 37(3), 263-8 (English) 1978. CODEN: JNENAD. ISSN: 0022-3069. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacodynamics) Dystrophic mice were treated for 5 wk beginning at 3 wk of age with 20 mg/day of pepstatin (I) [26305-03-3], a potent inhibitor of cathepsin D. Mortality was less and wt. gain greater in I treated mice than in controls. Muscle bulk was greater and hind lamb contractures were reduced in treated mice. Mean muscle fiber mass was significantly increased by I treatment. Inhibition of muscle protease may be the mechanism by which I slows the tempo of progression of mouse muscular dystrophy.
- Effects of protease inhibitors on the autolysis and protease activities of Antarctic krill
- Effects of protease inhibitors on the autolysis and protease activities of Antarctic krill. Kawamura, Yukio; Nishimura, Kimio; Matoba, Teruyoshi; Yonezawa, Daizo (Res. Inst. Food Sci., Kyoto Univ., Uji 611, Japan). Agric. Biol. Chem., 48(4), 923-30 (English) 1984. CODEN: ABCHA6. ISSN: 0002-1369. DOCUMENT TYPE: Journal CA Section: 17 (Food and Feed Chemistry) To det. which protease [9001-92-7] are responsible for the autolysis of krill, the effects of several protease inhibitors on the autolysis and protease activities of krill were investigated. Homogenates of whole bodies, and the cephalothorax and abdomen parts of frozen krill were equilibrated at 37° at different pHs between 2 to 10 and allowed to stand for 16 h, following which the increase in the TCA sol. fraction was monitored. 14C-Hb hydrolyzing activity was also measured using each homogenate as a crude enzyme prepn. The degree of autolysis and the 14C-Hb hydrolyzing activity were max. at pH 5-8 for the parts studied. The hydrolytic activity was highest in the cephalothorax, followed by that in the whole body and then the abdomen. The effects of inhibitors on the 14C-Hb hydrolyzing activity were examd. Soybean trypsin inhibitor (STI) [9078-38-0], diisopropyl fluorophosphate [55-91-4], and leupeptin inhibited the activity at neutral pH, and pepstatin [26305-03-3], monoiodoacetic acid [64-69-7], and leupeptin were effective at acidic pH for all the parts. Investigation of the effects of inhibitors on the autolysis at 20° at pH 4 and 7 by SDS-polyacrylamide gel electrophoresis indicated that the autolysis of the cephalothorax and whole body at pH 7 was suppressed a little by STI and the autolysis of the abdomen and whole body at pH 4 was significantly inhibited by iodoacetamide and leupeptin. Apparently, the main proteases responsible for the autolysis of krill are trypsin [9002-07-7] like-proteases at neutral pH and cathepsins (B [9047-22-7], H [60748-73-4], and L [60616-82-2] types) at acidic pH.
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