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Merck

B8385

Sigma-Aldrich

Bestatin hydrochloride

powder, ≥98% (HPLC)

Sinónimos:

N-[(2S,3R)-3-Amino-2-hydroxy-4-phenylbutyryl]-L-leucine hydrochloride

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About This Item

Fórmula empírica (notación de Hill):
C16H24N2O4 · HCl
Número de CAS:
Peso molecular:
344.83
Beilstein:
4628066
Número MDL:
Código UNSPSC:
12352202
ID de la sustancia en PubChem:
NACRES:
NA.77

product name

Bestatin hydrochloride, ≥98% (HPLC)

origen biológico

synthetic (organic)

Nivel de calidad

Análisis

≥98% (HPLC)

formulario

powder

mp

216 °C

solubilidad

water: 25 mg/mL, clear to very slightly hazy, colorless

espectro de actividad antibiótica

neoplastics

Modo de acción

enzyme | inhibits

temp. de almacenamiento

−20°C

cadena SMILES

O=C(N[C@@H](CC(C)C)C(O)=O)[C@@H](O)[C@H](N)CC1=CC=CC=C1.Cl[H]

InChI

1S/C16H24N2O4.ClH/c1-10(2)8-13(16(21)22)18-15(20)14(19)12(17)9-11-6-4-3-5-7-11;/h3-7,10,12-14,19H,8-9,17H2,1-2H3,(H,18,20)(H,21,22);1H/t12-,13+,14+;/m1./s1

Clave InChI

XGDFITZJGKUSDK-UDYGKFQRSA-N

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Descripción general

Chemical structure: amino acid derivatives

Acciones bioquímicas o fisiológicas

A metalloprotease inhibitor selective for aminopeptidase. Bestatin is a competitive and specific inhibitor of leucine aminopeptidase, aminopeptidase B, and triamino peptidase. It inhibits aminopeptidase B at 60 nM (using arginine-β-naphthylamide as substrate) and leucine aminopeptidase at 20 nM (leucine-β-naphthylamide as substrate). It showed no inhibition of aminopeptidase A, trypsin, chymotrypsin, elastase, papain, pepsin, or themolysin. It offers promise as a novel analgesic because it protects endogenous opioid peptides against degradation.

Nota de preparación

Solubility testing in water at 25 mg/ml yields a clear solution. Stock solutions at 1 mM are expected to be stable at least one month stored at -20 °C.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable

Equipo de protección personal

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Tina S Skinner-Adams et al.
Journal of medicinal chemistry, 50(24), 6024-6031 (2007-10-27)
Previous studies have pinpointed the M17 leucyl aminopeptidase of Plasmodium falciparum (PfLAP) as a target for the development of new antimalarials. This metallo-exopeptidase functions in the terminal stages of hemoglobin digestion and is inhibited by bestatin, a natural analog of
A Taylor
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 7(2), 290-298 (1993-02-01)
Aminopeptidases catalyze the cleavage of amino acids from the amino terminus of protein or peptide substrates. They are widely distributed throughout the animal and plant kingdoms and are found in many subcellular organelles, in cytoplasm, and as membrane components. Several
Hye Cheong Koo et al.
International journal of molecular sciences, 22(8) (2021-05-01)
It has been shown previously that a novel tetrapeptide, Arg-Leu-Tyr-Glu (RLYE), derived from human plasminogen inhibits vascular endothelial growth factor (VEGF)-induced angiogenesis, suppresses choroidal neovascularization in mice by an inhibition of VEGF receptor-2 (VEGFR-2) specific signaling pathway. In this study
Jian-Jun Gao et al.
Microvascular research, 82(2), 122-130 (2011-06-15)
Our previous study revealed that LYP, a bestatin dimethylaminoethyl ester, inhibited the growth of human ovarian carcinoma ES-2 xenografts in mice and suppressed aminopeptidase N (APN/CD13) activity more potently than bestatin. In this study, we examined the inhibitory effect of
Yu Wang et al.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(3), e21419-e21419 (2021-02-11)
In the early phase of the Coronavirus disease 2019 (COVID-19) pandemic, it was postulated that the renin-angiotensin-system inhibitors (RASi) increase the infection risk. This was primarily based on numerous reports, which stated that the RASi could increase the organ Angiotensin-converting

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