L6525

Sigma-Aldrich

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

≥97% (HPLC)

Empirical Formula (Hill Notation):
C49H83N15O13
CAS号:
分子量:
1090.28
MDL number:
PubChem Substance ID:
NACRES:
NA.32

Quality Level

assay

≥97% (HPLC)

storage temp.

−20°C

SMILES string

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

InChI key

MJGGTDHEIUOPEB-WBMHOGBOSA-N

Amino Acid Sequence

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

Application

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

Packaging

1 mg in glass bottle

Biochem/physiol Actions

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.

Substrates

Substrate for HIV protease.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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.
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...
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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