L-Argininol
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| Category | Others |
| Catalog number | BBF-04797 |
| CAS | |
| Molecular Weight | 160.20 |
| Molecular Formula | C6H16N4O |
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Specification
| Synonyms | (S)-1-(4-amino-5-hydroxypentyl)guanidine; H-Arg-ol |
| IUPAC Name | 2-[(4S)-4-amino-5-hydroxypentyl]guanidine |
| Canonical SMILES | C(CC(CO)N)CN=C(N)N |
| InChI | InChI=1S/C6H16N4O/c7-5(4-11)2-1-3-10-6(8)9/h5,11H,1-4,7H2,(H4,8,9,10)/t5-/m0/s1 |
| InChI Key | UFAABHKZLQFLSG-YFKPBYRVSA-N |
Reference Reading
1. Inhibition studies of some serine and thiol proteinases by new leupeptin analogues
R M McConnell, J L York, D Frizzell, C Ezell J Med Chem. 1993 Apr 16;36(8):1084-9. doi: 10.1021/jm00060a016.
Fifteen tripeptide analogues of leupeptin containing either a C-terminal argininal or lysinal were synthesized. The synthetic analogues were tested, using spectrophotometric assay techniques, as inhibitors of trypsin, kallikrein, thrombin, plasmin, and cathepsin B. The lysinal analogues were fairly selective as inhibitors of cathepsin B activity. Acetyl-L-leucyl-L-valyl-L-lysinal (21) showed a stronger inhibition of cathepsin B (IC50 = 4 nanomolar) than leupeptin. Acetyl-L-phenylalanyl-L-valyl-L-argininal (2i) was found to be a good inhibitor of cathepsin B (IC50 = 0.039 microM), thrombin (IC50 = 1.8 microM), and plasmin (IC50 = 2.2 microM).
2. Perturbation of neuronal cobalamin transport by lysosomal enzyme inhibition
Hua Zhao, Kalani Ruberu, Hongyun Li, Brett Garner Biosci Rep. 2014 Feb 1;34(1):e00092. doi: 10.1042/BSR20130130. Print 2014 Feb 1.
Cbl (cobalamin) utilization as an enzyme cofactor is dependent on its efficient transit through lysosomes to the cytosol and mitochondria. We have previously proposed that pathophysiological perturbations in lysosomal function may inhibit intracellular Cbl transport with consequences for down-stream metabolic pathways. In the current study, we used both HT1080 fibroblasts and SH-SY5Y neurons to assess the impact that protease inhibitors, chloroquine and leupeptin (N-acetyl-L-leucyl-L-leucyl-L-argininal), have on the distribution of [57Co]Cbl in lysosomes, mitochondria and cytosol. Under standard cell culture conditions the distribution of [57Co]Cbl in both neurons and fibroblasts was ~5% in lysosomes, 14% in mitochondria and 81% in cytosol. Treatment of cells with either 25 μM chloroquine or 40 μM leupeptin for 48 h significantly increased the lysosomal [57Co]Cbl levels, by 4-fold in fibroblasts and 10-fold in neurons, and this was associated with reduced cytosolic and mitochondrial [57Co]Cbl concentrations. Based on Western blotting of LAMP2 in fractions recovered from an OptiPrep density gradient, lysosomal Cbl trapping was associated with an expansion of the lysosomal compartment and an increase in a subpopulation of lysosomes with increased size and density. Moreover, the decreased mitochondrial Cbl that was associated with lysosomal Cbl trapping was correlated with decreased incorporation of [14C] propionate into cellular proteins/macromolecules, indicating an inhibition of Cbl-dependent Mm-CoA (methylmalonyl-coenzyme A) mutase activity. These results add support to the idea that lysosomal dysfunction may significantly impact upon Cbl transport and utilization.
3. Nostosins, Trypsin Inhibitors Isolated from the Terrestrial Cyanobacterium Nostoc sp. Strain FSN
Liwei Liu, Jouni Jokela, Matti Wahlsten, Bahareh Nowruzi, Perttu Permi, Yue Zhou Zhang, Henri Xhaard, David P Fewer, Kaarina Sivonen J Nat Prod. 2014 Aug 22;77(8):1784-90. doi: 10.1021/np500106w.
Two new trypsin inhibitors, nostosin A (1) and B (2), were isolated from a hydrophilic extract of Nostoc sp. strain FSN, which was collected from a paddy field in the Golestan Province of Iran. Nostosins A (1) and B (2) are composed of three subunits, 2-hydroxy-4-(4-hydroxyphenyl)butanoic acid (Hhpba), L-Ile, and L-argininal (1) or argininol (2). Nostosins A (1) and B (2) exhibited IC50 values of 0.35 and 55 μM against porcine trypsin, respectively, suggesting that the argininal aldehyde group plays a crucial role in the efficient inhibition of trypsin. Molecular docking of nostosin A (1) (449 Da), leupeptin (426 Da, IC50 0.5 μM), and spumigin E (610 Da, IC50 < 0.1 μM) with trypsin suggested prominent binding similarity between nostosin A (1) and leupeptin but only partial binding similarity with spumigin E. The number of hydrogen bonds between ligands and trypsin increased according to the length and size of the ligand molecule, and the docking affinity values followed the measured IC50 values. Nostosin A (1) is the first highly potent three-subunit trypsin inhibitor with potency comparable to the known commercial trypsin inhibitor leupeptin. These findings expand the known diversity of short-chain linear peptide protease inhibitors produced by cyanobacteria.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
