| Name, alias | Structure (click to show the formula) |
Composition formula (Mr) | IC50 (nM) |
Ki (nM) |
Maker | PN | pack- age (mg) |
Reference, note |
| Calpain Inhibitor I, MG-101 |
Ac-L-Leu-L-Leu-L-norleucinal file download => [.png] [.mol] |
C20H37N3O4 (383.53) | C1: 310; C2: 160; papain: 4,500; MMP2: 2.2x104 | C1: 86; C2: 192; papain: 2,200; CathB: 22; CathL: 0.5; trypsin: >5x105; proteasome: 6,000; thermolysin: >5x105; calcineurin /CaM: >2x105 | Bachem AG | N-1320 | 5, 25 | 1, 2, 3 |
| A. G. Scientific Inc. |
P-1153 | 5, 25 | ||||||
| Santa Cruz Biotech. Inc. |
SC-3089 | 0.5 | ||||||
| MERCK/Calbiochem | 208719 | 5, 25 | ||||||
| MERCK/Calbiochem | 208750 | 5 (in solution) | ||||||
| Sigma | A6185 | 5, 25 | ||||||
| Enzo/BioMol/Alexis | BML-P120 (ALX-260-037) | 5, 25 | ||||||
| Calpain Inhibitor II |
Ac-L-Leu-L-Leu-L-methional file download => [.png] [.mol] |
C19H35N3O4S (401.57) | C1: 250; C2: 140; papain: 3,600 | CathB: 100; CathL: 0.6 | Bachem AG | N-1315 | 5, 25 | 1 |
| A. G. Scientific Inc. |
C-1259 | 5, 25 | ||||||
| MERCK/Calbiochem | 208721 | 25 | ||||||
| Enzo/BioMol/Alexis | BML-PI100 (ALX-260-038) | 5 | ||||||
| Sigma | A6060 | 5, 25 | ||||||
| Calpain Inhibitor III, MDL-28170 | Z-L-Val-L- phenylalaninal file download => [.png] [.mol] |
C22H26N2O4 (382.46) | C1: 7; CathB: 25; trypsin: >2x106; plasmin: 2.7x105; kalikrein: >5x106 | Bachem AG | N-1535 | 25, 100 | 4, 5, 6 | |
| MERCK/Calbiochem | 208722 | 25 | ||||||
| Enzo/BioMol | BML-PI130 | 10, 50 | ||||||
| Sigma | M6690 | 25 | ||||||
| Calpain Inhibitor IV | Z-L-Leu-L-Leu -L-Tyr-CH2F file download => [.png] [.mol] |
C30H40N3O6F (557.66) |
C11: k2=2.9x104 M-1s-1; CathL: k2=6.8x105 M-1s-1 |
MERCK/Calbiochem | 208724 | 1 | 7, 8 A potent, cell-permeable, and irreversible inhibitor. |
|
| Kamiya Biomed. Co. (called "Calpain Inhibitor 1") | AB-050 | 3 | ||||||
| A. G. Scientific | C-1551 | 1 | ||||||
| "Calpain Inhibitor IV", MG-132 | Z-L-Leu-L-Leu -L-leucinal file download => [.png] [.mol] |
C26H41N3O5 (475.63) |
C2: 1,200; 20S proteasome: 100 | C2: 10; 20S proteasome: 6,900 | Bachem AG | N-1635 | 5, 25 | 9, 10, 11 |
| Calpain Inhibitor V | morpholinoureidyl -L-Val-L- homophenylalanyl -CH2F file download => [.png] [.mol] |
C21H30N3O4F (407.49) |
CathB: ～10; CathL: ～100 | MERCK/Calbiochem | 208726 | 1 | 12, 13 ca.70% inhibition of total cysteine protease activity from rat kidney by oral administration (10.0mg/kg) |
|
| Calpain Inhibitor VI, SJA6017 | 4-fluorophenyl sulfonyl-L-Val -L-leucinal file download => [.png] [.mol] |
C17H25N2O4SF (372.46) |
C1: 22; C2: 49; CathB: 6.9; CathL: 1.6; 20S proteasome: 105 | MERCK/Calbiochem | 208745 | 1, 5 | 14, 15, 16 | |
| Calpain Inhibitor X, AK275 | Z-L-Leu-L-Abu -CONH-C2H5 file download => [.png] [.mol] |
C21H31N3O5 (405.50) |
C1: 250; C2: 210; papain: 9.3x104; CathB: 2,400 | Alfa Aesar | J65826 | 1, 5 | 17, 18 A cell-permeable dipeptidyl α-ketoamide that acts as a potent, reversible, and active site inhibitor. |
|
| Calpain Inhibitor XI, AK295 | Z-L-Leu-L-Abu -CONH-(CH2)3 -morpholine file download => [.png] [.mol] |
C26H40N4O6 (504.63) |
C1: 140; C2: 41; CathB: 6,900 | MERCK/Calbiochem | 208743 | 1, 5 | 18 A cell-permeable dipeptidyl α-ketoamide that acts as a potent, highly selective, reversible, and active site inhibitor. |
|
| Calpain Inhibitor XII | Z-L-Leu-L -norvaline -CONH-CH2 -2-pyridyl file download => [.png] [.mol] |
C26H34N4O5 (482.58) |
C1: 19; C2: 120; CathB: 750 | Cayman Chemicals | 14466 | 1, 5, 10 | 18 A cell-permeable compound that acts as a potent, selective, reversible, and active site inhibitor. |
|
| Santa Cruz | sc-300318 | 1, 5 | ||||||
| Alfa Aesar | J64751 | 1, 5 | ||||||
| Funakoshi | 14466 | 1, 5, 10 | ||||||
| "Calpain Inhibitor 2" | Mu-Phe -HPh-CH2F |
C25H30O4N3F (455) |
Kamiya Biomed. Co. |
AB-051 | 5 | cross reactive to cathepsin L | ||
| Calpeptin | Z-L-Leu-L -norleucinal file download => [.png] [.mol] |
C20H30N2O4 (362.47) |
C1: 52; C2: 34; papain: 138; CathL: 138 | Proteasome: 1.1x105 Immunoproteasome: 1,000 | Enzo/BioMol/Alexis | BML-PI101 (ALX-260-014) | 10, 50 | 11, 19 |
| MERCK/Calbiochem | 03-34-0051 | 5, 25, 100 | ||||||
| Z-Leu-Tyr-CH2Cl | Z-Leu-Tyr -CH2Cl |
Bachem AG | N-1255 | 25, 100 | ||||
| Z-Phe-Tyr-CHO | Z-Phe-Tyr-CHO | Bachem AG | N-1540 | 25, 100 | ||||
| Z-Leu-Leu-CHO | Z-Leu -Leu-CHO |
362.5 | 1200 | BioMol | BML-PI116 | 5, 25 | 100-fold selective for calpain over proteasome | |
| Leupeptin | Ac-L-Leu-L -Leu-L-argininal file download => [.png] [.mol] |
C20H38N6O4 (426.56) |
C1: 351; C2: 176; papain: 1,500; CathB: 27 | C1: 320; C2: 430; CathB: 6; trypsin: 35; plasmin: 3,400; kalikrein: 1.9x105 | Bachem AG | N-1000 | 5, 25, 100 | 1, 4, 14, 16, 20, 21 |
| Peptide Inst. | 4041, 4041-v | 0.5 (vial), 25, 100, 1000 | ||||||
| Sigma | L2023 | 1, 5, 10, 25, 50, 100 | ||||||
| E-64 | [(2S,3S)-3 -carboxyoxirane-2 -carbonyl]-L-Leu- (4-guanidinobutyl) amide file download => [.png] [.mol] |
C15H27N5O5 (357.41) |
C1: 1,000; C2: 2,600; papain: 290; CathB: 800 | C11: 800 | Bachem AG | N-1645 | 5, 25 | 22, 23 |
| BioMol | ALX-260-007 (BML-PI105) | 5, 25 | ||||||
| MERCK/Calbiochem | 324890 | 1, 5, 25 | ||||||
| Peptide Inst. | 4096, 4096-v | 0.5 (vial), 25, 100, 1000 | ||||||
| E-64-c | [(2S,3S)-3 -carboxyoxirane-2 -carbonyl]-L-Leu -(3-methylbutyl)amide file download => [.png] [.mol] |
C15H26N2O5 (314.38) |
C11: 1.5x104; papain: 4,400; CathB: 240; CathL: 90 | C11: 960 | Bachem AG | N-1655 | 1, 5 | 23, 24, 25 Synthetic analog of E-64. |
| BioMol | BML-PI106 | 1 | ||||||
| Peptide Inst. | 4320-v | 5 | ||||||
| Sigma | E0514 | 1, 5 | ||||||
| E-64-d, EST, Loxistatin |
[(2S,3S)-3-ethoxy carbonyloxirane -2-carbonyl]-L-Leu -(3-methylbutyl)amide file download => [.png] [.mol] |
C17H30N2O5 (342.44) |
Bachem AG | N-1650 | 1, 5 | 24 A cell-permeable, irreversible inhibitor of cysteine proteases. Similar to E-64 but devoid of charged groups. The inhibitory activity of EST has been attributed to E-64c, the free acid formed by hydrolysis of the ester in vivo. |
||
| MERCK/Calbiochem | 330005 | 1 | ||||||
| Peptide Inst. | 4321-v | 5 | ||||||
| Sigma | E8640 | 0.25, 1 | ||||||
| PD150606 | 3-(4-iodophenyl)-2 -mercapto-(Z)-2 -propenoic acid file download => [.png] [.mol] |
C9H7O2SI (306.12) |
MMP2: 9,300 | C1: 210; C2: 370; papain: 1.5x105; CathB: 1.3x105; trypsin: 5x105; thermolysin: 2.0x105; calcineurin/CaM: 1.3x104 |
MERCK/Calbiochem | 513022 | 5 | 2, 3 A cell-permeable, non-competitive, selective non-peptide inhibitor. |
| PD151746 | 3-(5-fluoro- 3-indolyl)- 2-mercapto-(Z)- 2-propenoic acid file download => [.png] [.mol] |
C11H8NO2SF (237.25) |
C1: 260; C2: 5,300; papain: 5x105; CathB: 2x105; trypsin: 5x105; thermolysin: 5x105; calcineurin/CaM: 8.5x104 | MERCK/Calbiochem | 513024 | 5 | 2 A cell-permeable, non-competitive, selective non-peptide inhibitor. |
|
| PD145305 | 2-Mercapto-3- phenyl propanonic acid |
182.2 | Santa Cruz | sc-222131 | 5 | Negative control for PD150606 and PD151746. | ||
| Calpastatin, domain 1 |
134 aar | 14,208.52 | Takara | 7316 | 3 | 50 and 15 nM of calpastatin domain 1 inhibits, respectively, 100% and 50% of the activity of 7.5 µg/ml calpain-1 [µ-calpain]. | ||
| Ac- Calpastatin (184-210) |
Ac-DPMSSTYIEE LGKREVTIPP KYRELLA-NH2 |
3177.67 | Bachem AG | H-4076 | 0.5, 1 | |||
| Calpain inhibitor peptide (C-9181) |
DPMSSTYIEE LGKREVTIPP KTRELLA |
3136.56 | Sigma | C-9181 | 0.5 | |||
| AK269 | Z-L-Leu-L-Phe -CONH-C2H5 file download => [.png] [.mol] |
C26H33N3O5 (467.57) |
C1: 200; C2: 39; CathB: 4.5x104; CathL: 6,000 | - | 17, 18 | |||
| mCalp-I | Z-L-Leu-L-Abu -CONH-CH2 -C6H3-3,5 -(OCH3)2 file download => [.png] [.mol] |
C28H37N3O7 (527.62) |
C1: 2,300; C2: 22; CathB: 1,800 | C1: 940; C2: 25; CathB: - | - | 18, 26 | ||
| CEP-3122 | CH3-SO2-D -phenylmethyl serine-L -phenylalaninal file download => [.png] [.mol] |
C20H24N2O5S (404.49) |
C1: -; C2: -; papain: - | C1: 8; C2: 5; papain: 32 | - | 27, 28 | ||
| CEP-3453 | HSO3 addition of CEP-3122 file download => [.png] [.mol] |
C1: 8; CathB: 15 | C1: -; CathB: - | - | 28 | |||
| MDL104903 | [1-[(5-hydroxy- 4-phenylmethyl -3-oxazolidinyl) carbonyl]-2- ethylpropyl] carbamic acid phenylmethyl ester file download => [.png] [.mol] |
C23H28N2O5 (412.49) |
C1: - | C1: 33 | - | 29 | ||
| BDA-410 | (2S)-N-[(1S)-1-[(S) -hydroxy(3-oxo -2-phenyl-1- cyclopropen-1 -yl)methyl]-2- methylpropyl]-2- benzenesulfonyl amino-4-methyl pentanamide file download => [.png] [.mol] |
C26H32N2O5S (484.62) |
C1: 21; C2: 21; papain: 400; CathB: 1.6x105 | C1: 130; C2: 630; papain: -; CathB: -; thrombin, CathG, and proteasome: 1.0x105; CathD: 9.1x105 | - | 30, 31, 32 | ||
| SJA7019 | chloroacetic acid N'-[6,7-dichloro -4-(4-methoxy phenyl)-3-oxo -3,4-dihydro quinoxalin -2-yl]hydrazide file download => [.png] [.mol] |
C17H13N4O3Cl3 (427.67) |
C1: 77; C2: 64; CathL: 1,500 | C1: -; C2: -; papain: -; CathL: - | - | 33 | ||
| SJA7029 | chloroacetic acid N'-(6,7-dichloro -4-phenyl-3-oxo -3,4-dihydro quinoxalin -2-yl)hydrazide file download => [.png] [.mol] |
C16H11N4O2Cl3 (397.65) |
C1: 120; C2: 170; CathL: 4,200 | C1: -; C2: -; papain: -; CathL: - | - | 33 | ||
| SNJ1715 | (2S)-4-methyl -2-(3-phenyl thioureido)-N- [(3S)-tetrahydro -2-hydroxy -3-furanyl] pentanamide file download => [.png] [.mol] |
C17H25N3O3S (351.47) |
C1: 86; C2: 190; CathL: 4,200; 20S proteasome: >105 | C1: -; C2: - | - | 15 | ||
| SNJ1757 | (2S,5S)-5-benzyl -6-hydroxy-2-(2 -methylpropyl)-3 -morpholinone file download => [.png] [.mol] |
C15H21NO3 (263.34) |
C1: 700; C2: 930; CathB: >1x105 | C1: -; C2: -: CathB: - | - | 16 | ||
| SNJ1945 | [(1S)-1-([((1S)- 1-benzyl-3-(cyclo propylamino) -2,3-dioxopropyl) amino]carbonyl) -3-methylbutyl] carbamic acid 5-methoxy -3-oxapentyl ester file download => [.png] [.mol] |
C25H37N3O7 (491.58) |
C1: 170; C2: 99 | C1: -; C2: - | - | 34 | ||
| SNJ2008 | [(1S)-1-[([(1S) -1-benzyl-3- (cyclopropyl amino)-2,3-dioxo propyl]amino) carbonyl]-3- methylbutyl] carbamic acid 2-(pyridin-2-yl) ethyl ester file download => [.png] [.mol] |
C27H34N4O5 (494.59) |
C1: 29; C2: 17 | C1: -; C2: - | - | 35, 36 | ||
| A-705239, BSF 409425 | N-(1-carbamoyl -1-oxohex-1-yl)-2 -[E-2-(4-dimethyl aminomethyl phenyl)ethen-1- yl]benzamide file download => [.png] [.mol] |
C25H31N3O3 (421.54) |
C1: -; CathB: -; CathL: - | C1: 13 ;CathB: 27; CathL: 22; proteasome: 4.0x105 | - | 37, 38 | ||
| A-705253, BSF 419961, CAL 9961 | N-(1-benzyl-2- carbamoyl-2- oxoethyl)-2-[E- 2-(4-diethylamino methylphenyl) ethen-1-yl] benzamide file download => [.png] [.mol] |
C30H33N3O3 (483.61) |
C1: -; CathB: -; CathL: - | C1: 27 ;CathB: 62; CathL: 149; proteasome: 2.6x104 | - | 37, 38 | ||
| BN 82270 | phenothiazine- L-Leu-2-hydroxy tetrahydrofuran file download => [.png] [.mol] |
C25H29N3O5S (483.59) |
C1: >1,000; Cellular calpain inhibition: 1.3x104; Fe2+ induced lipid peroxidation in rat brain microsomes inhibition: 1.6x104 | - | 39, 40 Dual inhibitor for calpains (active after hydrolysis of the acetyl group) and lipid peroxidation. |
|||
| C-101, Myodur | L-aminocarnityl succinyl-L -Leu-L-argininal dichloride file download => [.png] [.mol] |
C23H47N7O6Cl2 (588.58) |
spectrin breakdown (145 kDa): 3.7x104 | - | 41 | |||
| C-201, Neurodur | L-cysteyl-L-Leu -L-argininal file download => [.png] [.mol] |
C15H30N6O6S (422.51) |
- | 42 No Ki or IC50 data. |
||||
| CYLA | diethyl acetal of C-201 file download => [.png] [.mol] |
C19H40N6O7S (496.63) |
- | 43 Active only after hydrolysis (=C-201). |
||||
| GABAdur | pregabalin- L-Leu- L-argininal file download => [.png] [.mol] |
C20H38N6O5 (442.56) |
- | 44 No Ki or IC50 data. |
||||
| Olesoxime, TRO19622 | (3Z)-N-hydroxy cholest-4-en -3-imine file download => [.png] [.mol] |
C27H45NO (399.66) |
mitochondrial translocator protein 18 kDa and its ligand, PK11195, binding: 3～5x104 | C1: **; C2: ** | - | 45, 46, 47 **Showing in vivo inhibitory activity. |
||
| Hypervalent organotellurium compound, RF19 | No.11 or RF19 file download => [.png] [.mol] |
C15H13OCl3Te (443.23) |
P. falciparum proteases: 200 | CathB: 7,900; CathL: 9,400; CathS: 2.0x105; CathK: 3.8x105 | - | 48, 49 | ||
| Macrocyclic aldehyde, CAT811 | ((7S,10S,13S) -7-formyl-10- isobutyl-9,12- dioxo-2-oxa- 8,11-diaza- bicyclo[13.2.2] nonadeca- 1(18),15(19), 16-trien-13-yl) -carbamic acid benzyl ester file download => [.png] [.mol] |
C29H37N3O6 (523.63) |
C1: 220; C2: 30; papain: >5x105; CathB: 70; pepsin and α-chymotrypsin: >5x105 |
- | 50 | |||
| Indole-containing 18-membered aldehyde | (S)-N-[(S)-4-methyl-1 -oxopentan-2-yl]-2, 16 -dioxo-3,20-diazabicyclo [15.2.1]icosa-l(19),17-diene -4-carbox amide file download => [.png] [.mol] |
C25H39N3O4 (445.60) |
C1: 42; C2: 66; α-chymotrypsin: >2.5x105 |
- | 51 | |||
| α-helical peptide | Ac-IPPKY CELLC-NH2 file download => [.png] [.mol] |
C64H96N12O14S2 (1321.67) |
C1: 1x104; papain: >1x105; CathB: >1x105;CathL: 3.9x104 | - | 52 | |||
| Dipeptidyl α,β-unsaturated ester | (E)-ethyl-4-(2-(benzyl-oxycarbonyl-amino)-4-methyl pentanamido)-5-phenylpent-2-enoate
file download => [.png] [.mol] |
C27H34N2O5 (466.58) |
P. falciparum growth rate in human erythrocytes: 5x103; HeLa cell growth: 3.5x105 | - | 53 | |||
| Macrocyclic β-turn peptide | c*[PGALK] file download => [.png] [.mol] |
C30H54N8O6 (622.81) |
C1: (～50%)***; C2: 1.7x104; papain: (～10%); CathL: (～100%) | - | 54
***showing relative values to inhibitory effect observed for C2 under the same condition. |
![[(2S,3S)-3-carboxyoxirane-2-carbonyl]-L-Leu-(4-guanidinobutyl)amide](images/e64_2d.png){kind=link}
![[(2S,3S)-3-carboxyoxirane-2-carbonyl]-L-Leu-(3-methylbutyl)amide](images/e64c_2d.png){kind=link}
![[(2S,3S)-3-ethoxycarbonyloxirane-2-carbonyl]-L-Leu-(3-methylbutyl)amide](images/e64d_2d.png){kind=link}
![[1-[(5-hydroxy-4-phenylmethyl-3-oxazolidinyl)carbonyl]-2-ethylpropyl]carbamic acidphenylmethyl ester](images/mdl104903_2d.png){kind=link}
![(2S)-N-[(1S)-1-[(S)-hydroxy(3-oxo-2-phenyl-1-cyclopropen-1-yl)methyl]-2-methylpropyl]-2-benzenesulfonylamino-4-methylpentanamide](images/bda-410_2d.png){kind=link}
![chloroacetic acidN'-[6,7-dichloro-4-(4-methoxyphenyl)-3-oxo-3,4-dihydroquinoxalin-2-yl]hydrazide](images/sja7019_2d.png){kind=link}
![(2S)-4-methyl-2-(3-phenylthioureido)-N-[(3S)-tetrahydro-2-hydroxy-3-furanyl] pentanamide](images/snj1715_2d.png){kind=link}
![[(1S)-1-([((1S)-1-benzyl-3-(cyclopropylamino)-2,3-dioxopropyl)amino]carbonyl)-3-methylbutyl]carbamic acid5-methoxy-3-oxapentyl ester](images/snj1945_2d.png){kind=link}
![[(1S)-1-[([(1S)-1-benzyl-3-(cyclopropylamino)-2,3-dioxopropyl]amino)carbonyl]-3-methylbutyl]carbamic acid2-(pyridin-2-yl)ethyl ester](images/snj2008_2d.png){kind=link}
![N-(1-carbamoyl-1-oxohex-1-yl)-2-[E-2-(4-dimethylaminomethylphenyl)ethen-1-yl]benzamide](images/a-705239_2d.png){kind=link}
![N-(1-benzyl-2-carbamoyl-2-oxoethyl)-2-[E-2-(4-diethylaminomethylphenyl)ethen-1-yl]benzamide](images/a-705253_2d.png){kind=link}
![[.png]](images/neurodur_2d.png){kind=link}
![((7S,10S,13S)-7-formyl-10-isobutyl-9,12-dioxo-2-oxa-8,11-diaza-bicyclo[13.2.2]nonadeca-1(18),15(19),16-trien-13-yl)-carbamic acid benzyl ester](images/cat811_2d.png){kind=link}
![(S)-N-[(S)-4-methyl-1-oxopentan-2-yl]-2, 16 -dioxo-3,20-diazabicyclo[15.2.1]icosa-l(19),17-diene-4-carboxamide](images/indole_containing_18membered_1c_2d.png){kind=link}
![c*[PGALK]](images/c-pgalk_2d.png){kind=link}
Z: benzyloxycarbonyl, Mu: morphlinoureidyl, HPh: homophenylalanyl, Abu, α-aminobutylic acid residue; Ac, acetyl; C1, calpain-1; C2, calpain-2; C11, chicken calpain-11; CathB/H/L, cathepsin B/H/L.
Notes:
*k2 indicates a rate constant (M-1s-1) of a reaction, E+I->EI (E: enzyme, I: inhibitor).
References:
- 1. Saito, M., Kawaguchi, N., Hashimoto, M., Kodama, T., Higuchi, N., Tanaka, T., Nomoto, K. & Murachi, T. Purification and structure of novel cysteine proteinase inhibitors, staccopins P1 and P2, from Staphylococcus tanabeensis. Agric. Biol. Chem. 51, 861-868, (1987).
- 2. Wang, K. K., Nath, R., Posner, A., Raser, K. J., Buroker-Kilgore, M., Hajimohammadreza, I., Probert, A. W., Jr., Marcoux, F. W., Ye, Q., Takano, E., Hatanaka, M., Maki, M., Caner, H., Collins, J. L., Fergus, A., Lee, K. S., Lunney, E. A., Hays, S. J. & Yuen, P. An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective. Proc. Natl. Acad. Sci. USA 93, 6687-6692, (1996).
- 3. Ali, M. A., Stepanko, A., Fan, X., Holt, A. & Schulz, R. Calpain inhibitors exhibit matrix metalloproteinase-2 inhibitory activity. Biochem. Biophys. Res. Commun. 423, 1-5, (2012).
- 4. Mehdi, S. Cell-penetrating inhibitors of calpain. Trends Biochem. Sci. 16, 150-153, (1991).
- 5. Mehdi, S., Angelastro, M. R., Wiseman, J. S. & Bey, P. Inhibition of the proteolysis of rat erythrocyte membrane proteins by a synthetic inhibitor of calpain. Biochem. Biophys. Res. Commun. 157, 1117-1123, (1988).
- 6. Lampi, K. J., Kadoya, K., Azuma, M., David, L. L. & Shearer, T. R. Comparison of cell-permeable calpain inhibitors and E64 in reduction of cataract in cultured rat lenses. Toxicol. Appl. Pharmacol. 117, 53-57, (1992).
- 7. Angliker, H., Anagli, J. & Shaw, E. Inactivation of calpain by peptidyl fluoromethyl ketones. J. Med. Chem. 35, 216-220, (1992).
- 8. Anagli, J., Hagmann, J. & Shaw, E. Investigation of the role of calpain as a stimulus-response mediator in human platelets using new synthetic inhibitors. Biochem. J. 274, 497-502, (1991).
- 9. Hayashi, M., Inomata, M., Saito, Y., Ito, H. & Kawashima, S. Activation of intracellular calcium-activated neutral proteinase in erythrocytes and its inhibition by exogenously added inhibitors. Biochim. Biophys. Acta 1094, 249-256, (1991).
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1. The original report was by Saito, M., Higuchi, N., Kawaguchi, N., Tanaka, T. and Murachi, T. at the 4th FAOB Congress in Singapore, November 30, 1986 (Abstracts of Papers, p58).
12. This reference described synthesis and the effect of morpholinoureidyl-L-Leu-L-homophenylalanyl-CH2F (mu-L-hF-fmk, P34089), but not those of Val (mu-V-hF-fmk, i.e., CI-V). Since the described method can be applied to mu-V-hF-fmk (CI-V) and no other reference describing the synthesis of CI-V was found, this reference is cited here.
17,18. The AK275 was first synthesized as a diastereometric mixture (called CX275); however, since a later study56 showed that the L, L isomer has inhibitory activity, this active structure is shown here, and so are for other AK series inhibitors.
20. In the original report, leupeptin was shown to have DL-argininal; however, a later study55 showed that L-argininal, but not D-argininal, has a strong affinity to trypsin. Thus, the structure is shown as Ac-L-Leu-L-Leu-L-argininal.
33. The original report was by Inoue, J., Cui, Y.-S., Sakai, O., Nakamura, M., Yuen, P.-W., and Wang, K.K.W. (1999) α-Substituted hydrazides having calpain inhibitory activity, in Proceedings of the FASEB Summer Conference on Calpains, 1999 June 20–23, Breckenridge, CO.
41. This reference did not mention about the stereochemical analysis, and, thus, the structure is an estimate from those of L-carnitine and leupeptin.
42. This reference did not mention about the stereochemical analysis, and, thus, the structure is an estimate from those of L-cysteic acid and leupeptin.
44. This reference did not mention about the stereochemical analysis, and, thus, the structure is an estimate from those of pregabalin and leupeptin.