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Key Documents

L6525

Sigma-Aldrich

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide

≥97% (HPLC)

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About This Item

Formula empirica (notazione di Hill):
C49H83N15O13
Numero CAS:
Peso molecolare:
1090.28
Numero MDL:
Codice UNSPSC:
12352202
ID PubChem:
NACRES:
NA.32

Livello qualitativo

Saggio

≥97% (HPLC)

Temperatura di conservazione

−20°C

Stringa SMILE

CCCC[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](Cc1ccc(cc1)[N+]([O-])=O)NC(=O)[C@H](CCCC)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCCN)C(C)C)C(N)=O

InChI

1S/C49H83N15O13/c1-7-9-15-33(40(52)67)58-41(68)29(6)57-44(71)36(22-23-38(65)66)60-47(74)37(26-30-18-20-31(21-19-30)64(76)77)62-45(72)34(16-10-8-2)61-48(75)39(27(3)4)63-46(73)35(17-13-25-55-49(53)54)59-42(69)28(5)56-43(70)32(51)14-11-12-24-50/h18-21,27-29,32-37,39H,7-17,22-26,50-51H2,1-6H3,(H2,52,67)(H,56,70)(H,57,71)(H,58,68)(H,59,69)(H,60,74)(H,61,75)(H,62,72)(H,63,73)(H,65,66)(H4,53,54,55)/t28-,29-,32-,33-,34-,35-,36-,37-,39-/m0/s1
MJGGTDHEIUOPEB-WBMHOGBOSA-N

Amino Acid Sequence

Lys-Ala-Arg-Val-Nle-pNO2-Phe-Glu-Ala-Nle-NH2

Applicazioni

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide has been used for measuring HIV (human immunodeficiency virus)-1 protease activity.

Azioni biochim/fisiol

Lys-Ala-Arg-Val-Nle-p-nitro-Phe-Glu-Ala-Nle amide is a synthetic substrate for HIV (human immunodeficiency virus)-1 protease and is commonly used for measuring HIV-1 protease activity.

Substrati

Substrate for HIV protease.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


Certificati d'analisi (COA)

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C Dash et al.
The Journal of biological chemistry, 276(4), 2487-2493 (2000-10-24)
The active site cleft of the HIV-1 protease (PR) is bound by two identical conformationally mobile loops known as flaps, which are important for substrate binding and catalysis. The present article reports, for the first time, an HIV-1 PR inhibitor
Yunfeng Tie et al.
The FEBS journal, 272(20), 5265-5277 (2005-10-13)
HIV-1 protease (PR) and two drug-resistant variants--PR with the V82A mutation (PR(V82A)) and PR with the I84V mutation (PR(I84V))--were studied using reduced peptide analogs of five natural cleavage sites (CA-p2, p2-NC, p6pol-PR, p1-p6 and NC-p1) to understand the structural and
L H Phylip et al.
Biochemical and biophysical research communications, 171(1), 439-444 (1990-08-31)
Kinetic constants (Km,Kcat) are derived for the hydrolysis of a number of chromogenic peptide substrates by the aspartic proteinase from HIV-2. The effect of systematic replacement of the P2 residue on substrate hydrolysis by HIV-1 and HIV-2 proteinases is examined.
Anita Fehér et al.
The Journal of general virology, 87(Pt 5), 1321-1330 (2006-04-11)
The protease (PR) of Murine leukemia virus (MLV) was expressed in Escherichia coli, purified to homogeneity and characterized by using various assay methods, including HPLC-based, photometric and fluorometric activity measurements. The specificity of the bacterially expressed PR was similar to
A D Richards et al.
The Journal of biological chemistry, 265(14), 7733-7736 (1990-05-15)
By replacement of the P1' residue in a capsid/nucleocapsid cleavage site mimic with 4-NO2-phenylalanine (Nph), an excellent chromogenic substrate, Lys-Ala-Arg-Val-Leu*Nph-Glu-Ala-Met, for HIV-1 proteinase (kappa cat = 20 s-1, Km = 22 microM) has been prepared. Substitution of the Leu residue

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