- A strategy combining quantitative reactions and reversible-covalent chemistry for sequential synthesis of sequence-controlled polymers with different sequences
-
A new strategy combing quantitative reactions and reversible-covalent chemistry is proposed for sequential synthesis of a series of sequence-controlled polymers with different sequences. Using a Michael addition reaction between acrylate and thiol, an aminolysis reaction of five-membered cyclic dithiocarbonate and a thiol substitution reaction of bromomaleimide and thiol, AB-, AB'C- and AB'CD-sequenced molecules are synthesized via AB, AB'C and AB'CD sequential monomer additions, respectively. These three molecules all have furan-protected maleimido group at one end, and the other end of AB-, AB'C- and AB'CD-sequenced molecules is amine, thiol and anthracene groups, respectively. Due to the fact that the furan-protected maleimido group can be efficiently transformed to maleimide group at high temperature via retro Diels-Alder reaction, AB-, AB'C- and AB'CD-sequenced molecules polymerize into sequence-controlled polymers with corresponding sequences at 120 °C. Through this strategy, the synthesis of molecular modules does not require separation and purification, and sequence-controlled polymers with specific sequence can be synthesized in a one-pot process via adding different monomers and adjusting reaction condition.
- Xu, Chao-Ran,Zhang, Ze,Pan, Cai-Yuan,Hong, Chun-Yan
-
p. 294 - 304
(2019/04/25)
-
- NOVEL ARYLALKENE DERIVATIVES AND USE THEREOF AS SELECTIVE ESTROGEN RECEPTOR MODULATORS
-
The invention provides novel ethylene derivatives represented by Formula I, which may be used as selective estrogen receptor modulators (SERMs) and useful in the prophylaxis and/or treatment of estrogen-dependent conditions or conditions.
- -
-
Paragraph 0237; 0313
(2013/07/19)
-
- Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications
-
Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.
- Chalker, Justin M.,Lercher, Lukas,Rose, Nathan R.,Schofield, Christopher J.,Davis, Benjamin G.
-
supporting information; experimental part
p. 1835 - 1839
(2012/04/04)
-
- Reversible inactivation of bovine plasma amine oxidase by cysteamine and related analogs
-
Cysteamine (1) was reported many years ago to reversibly inhibit lentil seedling amine oxidase, through the formation of a complex with thioacetaldehyde, the turnover product of 1. Herein, cysteamine (1) and its analogs 2-(methylamino)ethanethiol (3) and 3-aminopropanethiol (6) were found to be reversible inhibitors of bovine plasma amine oxidase (BPAO), but 2-(methylthio)ethylamine (7) was determined to be a weak irreversible inhibitor of BPAO. Based on our results, indicating the necessity of a sulfhydryl-amine for reversible inactivation of BPAO, the failure of inhibited BPAO to recover activity after gel filtration, the first-order kinetics of activity recovery upon dialysis, and 2,4,6-trihydroxyphenylalanine quinine (TPQ) cofactor transformation which indicated from the results of phenylhydrazine titration and substrate protection, we propose a mechanism for the reversible inactivation of BPAO by 1 involving the formation of a cofactor adduct, thiazolidine, between BPAO and 1.
- Jeon, Heung Bae,Jang, Yujin
-
experimental part
p. 442 - 446
(2011/10/12)
-
- Versatile synthesis of secondary 2-amino thiols and/or their disulfides via thiazolinium salts
-
Commercially available β-amino alcohols have been transformed into various secondary β-amino thiols and/or their disulfides by using methyl dithioacetate as a source of sulfur. The transformation involves a thiazolinium salt as a versatile key intermediate, which enables easy modulation of the product structure by varying the substituents on the hetero-cycle and the N-alkylating agent.
- Mercey, Guillaume,Lohier, Jean-Francois,Gaumont, Annie-Claude,Levillain, Jocelyne,Gulea, Mihaela
-
experimental part
p. 4357 - 4364
(2011/02/24)
-
- Facile conversion of cysteine and alkyl cysteines to dehydroalanine on protein surfaces: Versatile and switchable access to functionalized proteins
-
An efficient and robust oxidative elimination of cysteine to dehydroalanine has been discovered. The reaction is induced by O-mesitylenesulfonylhydroxylamine (MSH) and is compatible with methionine. The key elimination has been executed on protein surfaces and allows ready access to different post-translationally modified proteins through conjugate addition of sulfur nucleophiles to dehydroalanine. Treatment of the resulting thioether with MSH results in regeneration of dehydroalanine, allowing a "functional switch" by subsequent addition of a different thiol. Copyright
- Bernardes, Goncalo J. L.,Chalker, Justin M.,Errey, James C.,Davis, Benjamin G.
-
p. 5052 - 5053
(2008/10/09)
-
- Reductive Opening of the Thiazolidine Ring. Selective N-Methylation of Cysteamines
-
The reaction of thiazolidines 2 and 7 with borane was investigated.It gave N-methylcysteamines 3 and 8 through thiazolidine ring opening.Sodium borohydride and lithium aluminum hydride were ineffective.
- Melchiorre, Carlo,Giardina, Dario,Angeli, Piero
-
p. 1215 - 1216
(2007/10/02)
-