3D-VAA-14568 - abz-irtpp3-tyr-no2-nh2

<p>M06085 - Fmoc-2-Abz-OH</p>

<p>Bachem ID: 4002711.</p>

Fluorogenic (FRET) substrate for angiotensin I-converting enzyme (ACE). Enzymatic cleavage of Abz-Gly-Nph-Pro yields Abz-Gly-OH emitting at 420 nm.

A fluorogenic substrate for neutral metalloendopeptidases, e.g. Pseudomonas aeruginosa elastase, enkephalinase (NEP 24.11), and thermolysin. Abz-AGLA-Nba is also cleaved by atrolysin B and C.

Fluorogenic cleavage product of ACE substrate Abz-Gly-p-nitro-Phe-Pro.

Efficient fluorogenic substrate for two matrix metalloproteinases: interstitial collagenase (MMP-1) and gelatinase (MMP-9). Dnp-Pro-Cha-Gly-Cys(Me)-His-Ala-Lys(N-Me-Abz)-amide has favorable solubility characteristics. Both enzymes cleave this substrate between Gly and Cys(Me) (Smc), liberating a cleavage product with a fluorescence signal suitable for inhibitor screening and determining Ki values. The major advantage of this FRET substrate is its adaptability to filters commonly available on commercial plate readers (excitation at 365 nm and emission at 450 nm).

<p>Bachem ID: 4025576.</p>

The water-soluble peptidylhydroxamic acid FN439 is a broad-spectrum inhibitor of human matrix metalloproteinases. 4-Abz-Gly-Pro-D-Leu-D-Ala-NHOH retains its activity even after prolonged incubation with pronase or human granulocyte elastase. FN 439 inhibits interstitial and granulocyte collagenases, granulocyte gelatinase and skin fibroblast stromelysin with IC₅₀ of 1 · 10⁻⁶ M, 3 · 10⁻⁵ M and 1.5 · 10⁻⁴ M, respectively.

Internally quenched fluorogenic peptide substrate containing anthranilic acid as fluorescent donor and m-nitro-tyrosine as acceptor (quencher). The sequence Abz-RVKRGLAY(NO₂)E is based on the sequence of hemagglutinin. The FRET substrate is efficiently cleaved by furin, a subtilisin-like eukaryotic serine endoprotease with Km = 3.8 µM and kcat = 29.3 s-¹ (kcat/Km = 7’710’000 M-¹s-¹). Its kcat/Km value is over 2000-fold higher than that of the commonly used substrate Boc-Arg-Val-Arg-Arg-AMC (I-1645). FRET Substrate for the basic residue-specific yeast aspartyl protease yapsin 1.

Potent inhibitor of the Ras farnesyltransferase (Ftase) with an IC₅₀ of 50 nM. It prevented farnesylation of Ras and resulted in its inability to associate with other cell signaling components at the interior of the plasma membrane microenvironment.

Useful as spacer in SPPS.

Internally quenched fluorogenic (FRET) substrate which allows aminopeptidase P (APP) activity determination by a continuous fluorescent assay (kcat/Km = 29’000 M⁻¹s⁻¹ for E.coli APP and kcat/Km = 1’142’000 M⁻¹s⁻¹ for rat APP).

Fmoc-Lys(Boc-Abz)-OH a protected building block for the preparation of fluorescence-labeled peptides. The anthranilic acid attached at the side-chain of lysine is highly sensitive and its fluorescence spectrum does not overlap with those of Trp, Phe, and Tyr.

<p>Bachem ID: 4028486.</p>

Abz-AFAFDVY(NO₂)D, a fluorogenic (FRET) substrate for endoproteinase AspN, Asp-specific proteases from Staphylococcus aureus, Bacillus licheniformis and Streptomyces griseus.

Excellent angiotensin I-converting enzyme (ACE) FRET substrate with a Km value of 4.0 µM and a kcat value of 210 s⁻¹. Alves et al. developed a continuous fluorescent assay using Abz-FRK(Dnp)P for the determination of ACE activity in plasma and tissue.

Abz-GIVRAK(Dnp), a very efficient and selective FRET substrate for human cathepsin B (Km = 5.9 µM, kcat = 43 s⁻¹, kcat/Km = 7288 mM⁻¹s⁻¹). The kcat/Km values for cathepsin K, L, V, X, and cruzain were 133.3, 100, 32, 17, and 75 mM⁻¹s⁻¹, respectively.

Specific inhibitor of thimet oligopeptidase (soluble metalloendopeptidase, EC 3.4.24.15) (Ki = 0.027 ± 0.003 µM). Neprilysin (Endopeptidase-2, EC 3.4.24.11) converts Cpp-AAF-pAb into a potent inhibitor of angiotensin-converting enzyme (ACE).

Selective substrate for angiotensin-converting enzyme 2 (ACE2), an ACE homolog which differs in its specificity and physiological role from ACE. The internally quenched fluorescent (FRET) substrate is potentially useful in applications such as high-throughput screening of ACE2 inhibitors (Km = 23 µM, kcat/Km = 3.5 · 10⁴ M⁻¹s⁻¹).