77237-89-9Relevant articles and documents
RAFT polymerization and self-assembly of thermoresponsive poly(N-decylacrylamide-b-N,N-diethylacrylamide) block copolymers bearing a phenanthrene fluorescent α-end group
Prazeres, Telmo J.V.,Beija, Mariana,Charreyre, Marie-Thérèse,Farinha, José Paulo S.,Martinho, José M.G.
, p. 355 - 367 (2010)
Phenanthrene α-end-labeled poly(N-decylacrylamide-b-N,N-diethylacrylamide) (PDcAn-b-PDEAm) block copolymers consisting in a highly hydrophobic block (n = 11) and a thermoresponsive block with variable length (79 ≤ m ≤ 468) were synthesized by reversible addition-fragmentation chain transfer (RAFT) polymerization. A new phenanthrene-labeled chain transfer agent (CTA) was synthesized and used to control the RAFT polymerization of a hydrophobic acrylamide derivative, N-decylacrylamide (DcA). This first block was further used as macroCTA to polymerize N,N-diethylacrylamide (DEA) in order to prepare diblock copolymers with the same hydrophobic block of PDcA (number average molecular weight: Mn = 2720 g mol-1, polydispersity index: Mw/Mn = 1.13) and various PDEA blocks of several lengths (Mn = 10,000-60,000 g mol-1) with a very high blocking efficiency. The resulting copolymers self-assemble in water forming thermoresponsive micelles. The critical micelle concentration (CMC) was determined using Fo?rster resonance energy transfer (FRET) between phenanthrene linked at the end of the PDcA block and anthracene added to the solution at a low concentration (10-5 M), based on the fact that energy transfer only occurs when phenanthrene and anthracene are located in the core of the micelle. The CMC (～2 μM) was obtained at the polymer concentration where the anthracene fluorescence intensity starts to increase. The size of the polymer micelles decreases with temperature increase around the lower critical solution temperature of PDEA in water (LCST ～ 32 °C) owing to the thermoresponsiveness of the PDEA shell.
Alkyl perchlorates in the Ritter-type reaction. Synthesis of N-alkylamides
Yashin,Markov,Sedenkova,Vasilenko,Grishin, Yu. K.,Kuznetsova,Averina
, p. 980 - 985 (2020/06/17)
The Ritter-type reaction of alkyl perchlorates with nitriles of various structures was systematically studied. The reaction has a wide scope and proceeds under extremely mild conditions without any catalysts or special activation of reagents. A structural diversity of the obtained by the Ritter-type reaction N-alkyl amides bearing small ring, double bonds, additional functional groups, aromatic and adamantane fragments, was demonstrated.
COMPOSITIONS AND METHODS FOR INHIBITING RETICULON 4
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Paragraph 0645; 0647; 0711, (2018/08/26)
Disclosed herein, inter alia, are compositions and methods useful for inhibiting reticulon 4(RTN4).
Chemoproteomics-enabled covalent ligand screen reveals a cysteine hotspot in reticulon 4 that impairs ER morphology and cancer pathogenicity
Bateman,Nguyen,Roberts,Miyamoto,Ku,Huffman,Petri,Heslin,Contreras,Skibola,Olzmann,Nomura
supporting information, p. 7234 - 7237 (2017/07/11)
Chemical genetics has arisen as a powerful approach for identifying novel anti-cancer agents. However, a major bottleneck of this approach is identifying the targets of lead compounds that arise from screens. Here, we coupled the synthesis and screening of fragment-based cysteine-reactive covalent ligands with activity-based protein profiling (ABPP) chemoproteomic approaches to identify compounds that impair colorectal cancer pathogenicity and map the druggable hotspots targeted by these hits. Through this coupled approach, we discovered a cysteine-reactive acrylamide DKM 3-30 that significantly impaired colorectal cancer cell pathogenicity through targeting C1101 on reticulon 4 (RTN4). While little is known about the role of RTN4 in colorectal cancer, this protein has been established as a critical mediator of endoplasmic reticulum tubular network formation. We show here that covalent modification of C1101 on RTN4 by DKM 3-30 or genetic knockdown of RTN4 impairs endoplasmic reticulum and nuclear envelope morphology as well as colorectal cancer pathogenicity. We thus put forth RTN4 as a potential novel colorectal cancer therapeutic target and reveal a unique druggable hotspot within RTN4 that can be targeted by covalent ligands to impair colorectal cancer pathogenicity. Our results underscore the utility of coupling the screening of fragment-based covalent ligands with isoTOP-ABPP platforms for mining the proteome for novel druggable nodes that can be targeted for cancer therapy.
