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Merck

B8385

Sigma-Aldrich

Bestatin -hydrochlorid

powder, ≥98% (HPLC)

Synonym(e):

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

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About This Item

Empirische Formel (Hill-System):
C16H24N2O4 · HCl
CAS-Nummer:
Molekulargewicht:
344.83
Beilstein:
4628066
MDL-Nummer:
UNSPSC-Code:
12352202
PubChem Substanz-ID:
NACRES:
NA.77

product name

Bestatin -hydrochlorid, ≥98% (HPLC)

Biologische Quelle

synthetic (organic)

Assay

≥98% (HPLC)

Form

powder

mp (Schmelzpunkt)

216 °C

Löslichkeit

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

Wirkungsspektrum von Antibiotika

neoplastics

Wirkungsweise

enzyme | inhibits

Lagertemp.

−20°C

SMILES String

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

InChIKey

XGDFITZJGKUSDK-UDYGKFQRSA-N

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Allgemeine Beschreibung

Chemical structure: amino acid derivatives

Biochem./physiol. Wirkung

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.

Angaben zur Herstellung

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.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, type N95 (US)


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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
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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
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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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