72284-86-7

Basic information

• Product Name: 8-bromooctanoic acid benzyl ester
• Synonyms: 8-bromooctanoic acid benzyl ester
• CAS NO: 72284-86-7
• Molecular Weight: 313.235
• Mol File: 72284-86-7.mol

Chemical Properties

• CAS DataBase Reference: 8-bromooctanoic acid benzyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: 8-bromooctanoic acid benzyl ester(72284-86-7)
• EPA Substance Registry System: 8-bromooctanoic acid benzyl ester(72284-86-7)

Safety Data

• Hazardous Substances Data: 72284-86-7(Hazardous Substances Data)

Upstream product

• 17696-11-6 8-bromooctanoic acid 
• 100-51-6 benzyl alcohol 
• 100-39-0 benzyl bromide 

Downstream Products

• 1031704-68-3 5-[4-(7-benzyloxycarbonyl-heptyloxy)-phenyl]-isoxazole-3-carboxylic acid tert-butyl ester 
• 1552321-98-8 7-(benzyloxycarbonyl)heptyl 5-(Cbz-amino)-4-oxopentanoate 

Relevant articles and documents

Functionally Versatile and Highly Stable Chelator for 111In and 177Lu: Proof-of-Principle Prostate-Specific Membrane Antigen Targeting

Here, we present the synthesis and characterization of a new potentially nonadentate chelator H4pypa and its bifunctional analogue tBu4pypa-C7-NHS conjugated to prostate-specific membrane antigen (PSMA)-targeting peptidomimetic (Glu-urea-Lys). H4pypa is very functionally versatile and biologically stable. Compared to the conventional chelators (e.g., DOTA, DTPA), H4pypa has outstanding affinities for both 111In (EC, t1/2 ≈ 2.8 days) and 177Lu (β-,?, t1/2 ≈ 6.64 days). Its radiolabeled complexes were achieved at >98% radiochemical yield, RT within 10 min, at a ligand concentration as low as 10-6 M, with excellent stability in human serum over at least 5-7 days (- complexes (M3+ = In3+, Lu3+, La3+) were dependent on the ionic radii, where the smaller In3+ has the highest pM value (30.5), followed by Lu3+ (22.6) and La3+ (19.9). All pM values are remarkably higher than those with DOTA, DTPA, H4octapa, H4octox, and H4neunpa. Moreover, the facile and versatile bifunctionalization enabled by the p-OH group in the central pyridyl bridge of the pypa scaffold (compound 14) allows incorporation of a variety of linkers for bioconjugation through easy nucleophilic substitution. In this work, an alkyl linker was selected to couple H4pypa to a PSMA-targeting pharmacophore, proving that the bioconjugation sacrifices neither the tumor-targeting nor the chelation properties. The biodistribution profiles of 111In- and 177Lu-labeled tracers are different, but promising, with the 177Lu analogue particularly outstanding.

Synthesis and biodistribution studies of 99mTc labeled fatty acid derivatives prepared via “Click approach” for potential use in cardiac imaging

123I-Iodophenylpentadecanoic acid (IPPA) is a metabolic agent used in nuclear medicine for diagnosis of myocardial defects. Efforts are underway worldwide to develop a 99mTc substitute of the above radiopharmaceutical for the aforementioned application. Herein, we report synthesis and biodistribution studies of 99mTc labeled fatty acids (8, 11, and 15 carbons) obtained via “click chemistry” for its potential use in myocardial imaging. ω-Bromo fatty acids (8C/11C/15C) were synthetically modified at bromo terminal to introduce a heterocyclic triazole with glycine sidearm in a five step procedure. Modified fatty acids were subsequently radiolabeled with preformed [99mTc(CO)3]+ synthon to yield the desired fatty acid complexes which were evaluated in Swiss mice. All the radiolabeled complexes were obtained with radiochemical purities >80%, as characterized by HPLC. Biodistribution studies of all three complexes in Swiss mice showed myocardial uptake of ~6-9% ID/g at 2?minutes post-injection, close to*I-IPPA (~9% ID/g). Complexes exhibited significant retention in the myocardium up to 30?minutes (~1% ID/g) but were lower to the standard agent (~7% ID/g). Similar uptake of activity in myocardium for the newly synthesized complexes in comparison to 125I-IPPA along with favorable in vivo pharmacokinetics merits potential for the present “click” design of complexes for myocardial imaging.

Cationic Lipid

The present invention provides a cationic lipid which is able to be used for nucleic acid delivery to the cytoplasm. A cationic lipid according to the present invention is, for example, a compound represented by formula (1) or a pharmaceutically acceptable salt thereof, wherein L1 and L2 independently represent an alkylene group having 3 to 10 carbon atoms; R1 and R2 independently represent an alkyl group having 4 to 24 carbon atoms or an alkenyl group having 4 to 24 carbon atoms; R3 represents an alkyl group having 1 to 3 carbon atoms; and X1 represents a single bond or CO—O—.

CATIONIC LIPID

The present invention provides a cationic lipid which is able to be used for nucleic acid delivery to the cytoplasm. A cationic lipid according to the present invention is, for example, a compound represented by formula (1a) or a pharmaceutically acceptable salt thereof. (In formula (1a), each of L1 and L2 independently represent an alkylene group having 3-10 carbon atoms; each of R1 and R2 independently represent an alkyl group having 4-22 carbon atoms or an alkenyl group having 4-22 carbon atoms; X1 represents a single bond or -CO-O-; and ring P represents one of formulae (P-1) to (P-5).)(In formulae (P-1) to (P-5), R3 represents an alkyl group having 1-3 carbon atoms.)

Development of Bifunctional Inhibitors of Polo-Like Kinase 1 with Low-Nanomolar Activities Against the Polo-Box Domain

Polo-like kinase 1 (Plk1), a validated cancer target, harbors a protein-protein interaction domain referred to as the polo-box domain (PBD), in addition to its enzymatic domain. Although functional inhibition either of the enzymatic domain or of the PBD has been shown to inhibit Plk1, so far there have been no reports of bifunctional agents with the potential to target both protein domains. Here we report the development of Plk1 inhibitors that incorporate both an ATP-competitive ligand of the enzymatic domain, derived from BI 2536, and a functional inhibitor of the PBD, based either on the small molecule poloxin-2 or on a PBD-binding peptide. Although these bifunctional agents do not seem to bind both protein domains simultaneously, the most potent compound displays low-nanomolar activity against the Plk1 PBD, with excellent selectivity over the PBDs of Plk2 and Plk3. Our data provide insights into challenges and opportunities relating to the optimization of Plk1 PBD ligands as potent Plk1 inhibitors.

Solid-phase assembly and in situ screening of protein tyrosine phosphatase inhibitors

(Chemical Equation Presented) A highly efficient solid-phase strategy for assembly of small molecule inhibitors against protein tyrosine phosphatase 1B (PTP1B) is described. The method is highlighted by its simplicity and product purity. A 70-member combinatorial library of analogues of a known PTP1B inhibitor has been synthesized, which upon direct in situ screening revealed a potent inhibitor (Ki = 7.0 μM) against PTP1B.