359014-82-7

Upstream product

• 16654-54-9 6-phenoxyhexan-1-ol 
• 98-59-9 p-toluenesulfonyl chloride 
• 629-11-8 1,6-hexanediol 
• 75351-33-6 (6-hydroxyhexyl)tosylate 
• 629-03-8 1 ,6-dibromohexane 
• 108-95-2 phenol 
• 51795-97-2 6-bromohexyloxybenzene 
• 16836-95-6 silver(I) 4-methylbenzenesulfonate 

Downstream Products

• 359014-83-8 2-(6-phenoxyhexyl)-1H-isoindole-1,3(2H)-dione 
• 16728-68-0 6-phenoxyhexan-1-amine 

Relevant academic research and scientific papers

Single-Site Labeling of Native Proteins Enabled by a Chemoselective and Site-Selective Chemical Technology

Chemical biology research often requires precise covalent attachment of labels to the native proteins. Such methods are sought after to probe, design, and regulate the properties of proteins. At present, this demand is largely unmet due to the lack of empowering chemical technology. Here, we report a chemical platform that enables site-selective labeling of native proteins. Initially, a reversible intermolecular reaction places the "chemical linchpins" globally on all the accessible Lys residues. These linchpins have the capability to drive site-selective covalent labeling of proteins. The linchpin detaches within physiological conditions and capacitates the late-stage installation of various tags. The chemical platform is modular, and the reagent design regulates the site of modification. The linchpin is a multitasking group and facilitates purification of the labeled protein eliminating the requirement of additional chromatography tag. The methodology allows the labeling of a single protein in a mixture of proteins. The precise modification of an accessible residue in protein ensures that their structure remains unaltered. The enzymatic activity of myoglobin, cytochrome C, aldolase, and lysozyme C remains conserved after labeling. Also, the cellular uptake of modified insulin and its downstream signaling process remain unperturbed. The linchpin directed modification (LDM) provides a convenient route for the conjugation of a fluorophore and drug to a Fab and monoclonal antibody. It delivers trastuzumab-doxorubicin and trastuzumab-emtansine conjugates with selective antiproliferative activity toward Her-2 positive SKBR-3 breast cancer cells.

Aldehydes can switch the chemoselectivity of electrophiles in protein labeling

We show that the chemoselectivity of an electrophile in protein labeling can be promiscuous. An aldehyde enables switching of chemoselectivity of an epoxide and a sulfonate ester along with an enhanced rate of reaction. The chemical technology renders single-site installation of diverse probes on a protein and delivers analytically pure tagged proteins.

Self-assembly and dynamics of [2]- and [3]rotaxanes with a dinuclear macrocycle containing reversible Os-N coordinate bonds

With a dinuclear macrocycle 2 that contains weak reversible OsVI-N coordinate bonds, self-assembly and equilibrium dynamics of [2]- and [3]rotaxanes have been investigated. When the macrocycle 2 was mixed together with threads 4a-e, which all contain an adipamide station but different sizes of end groups, [2]pseudorotaxane- and rotaxane-like complexes were immediately formed with large association constants > of 7 × 103M-1 in CDCl3 at 298 K. Exchange dynamics, explored by 2D-EXSY experiments, suggest that assembly and disassembly of complexes occur through two distinct pathways, slipping or clipping, and this depends on the size of the end groups. The slipping pathway is predominant with smaller end groups that give pseudorotaxane-like complexes, while the clipping pathway is observed with larger end groups that yield rotaxane-like complexes. Under the same conditions, exchange barriers (ΔG≠) were 14.3 kcal mol-1 for 4a and 16.7 kcal mol-1 for 4d, and indicate that the slipping process is at least one order of magnitude faster than the clipping process. Using threads 13a and 13b that contain two adipamide groups, more complicated systems have been investigated in which [2]rotaxane, [3]rotaxane, and free components are in equilibrium. Concentration- and temperature-dependent 1H NMR spectroscopic studies allowed the identification of all possible elements and the determination of their relative distributions in solution. For example, the relative distribution of the free components, [2]rotaxane, and [3]rotaxane are 30, 45, and 25%, respectively, in a mixture of 2 (2mM) and 13a (2mM) in CDCl3, at 10°C. However, [3]rotaxane exists nearly quantitatively in a mixture of 2 (4mM) and 13a (2mM) in CDCl3 at a low temperature - 10°C.