• YAKHAK HOEJI
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• v.31 no.1
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• pp.40-41
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• 1987

4-Hydroxy-2H-1, 2-benzothiazine-3-carboxylic acid 1a was reacted with 2 equivalents of dicyclohexylcarbodiimide (DCC) to give 2-cyclohexyl-3-cyclohexylimino-4,5-dihydro-1H-imidazo [1,5-b][1,2] benzothiazine-10, 10a-dyhydro-1,10-dione 5,5-dioxide 2a and dicyclohexylurea (DCU). On the other hand 2-substituted-4-hydroxy-2H-1, 2-benzothiazine-3-carboxylic acid 1,1-dioxide 1b or c was reacted with DCC to give 2-cyclohexylimino-3-cyclohexyl-5-alkyl-4-oxo-2,5H-1,3-oxazino [5,6-c]-1,2-benzothiazine 6,6-dioxide 2b or c and DCU.

• Bulletin of the Korean Chemical Society
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• v.22 no.11
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• pp.1270-1272
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• 2001

• YAKHAK HOEJI
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• v.38 no.1
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• pp.1-5
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• 1994

We have synthesized some 2-(2-benzyloxybenzoyloxy)-and 2-(2,6-dibenzyloxybenzoyloxy)-acetophenones as intermediates for flavone synthesis. The reaction of polyoxygenated 2-hydroxyacetophenones with 2-benzyloxybenzoic acid or 2,6-dibenzyloxybenzoic acid in the presence of dicyclohexylcarbodiimide and p-dimethylaminopyridine resulted in a good yield$(70{\sim}89%)$ of 2-(2-benzyloxybenzoyloxy)-acetophenones or 2-(2,6-dibenzyloxybenzoyloxy) acetophenones under milder conditions and in shorter time than the previous methods. This new methods using benzoic acids instead of benzoyl chlorides saves one reaction step of acid chlorination in comparision of the previous methods.

• Journal of the Korean Chemical Society
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• v.38 no.5
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• pp.382-390
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• 1994

New 6-imino-5H-benzimidazo[2,1-b][1,3,5]benzothiadiazepine derivatives (8) were successfully synthesized in good yields from the N-[2-(benzimidazol-2-yl thio)phenyl]thiourea derivatives (6) in the presence of dicyclohexylcarbodiimide(DCC) and from N-[2-(benzimidazol-2-yl thio)phenyl]-S-methylisothiourea derivatives (7) with potassium carbonate.

• Applied Chemistry for Engineering
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• v.22 no.3
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• pp.319-322
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• 2011

N,N'-Dicyclohexylcarbodiimide (DCC) known as powerful dehydrating reagent in amide or ester synthesis is converted into N,N'-dicyclohexylurea (DCU) during the reaction. In the paper, DCU was recovered from the reaction for the synthesis of the hydrophilic derivative of ${\beta}$-sitosterol, and the purification of the recovered DCU and the dehydration of DCU into DCC were investigated. In the presence of tosyl chloride, (TsCl) and triethylamine (TEA), DCU was converted into DCC, and the optimum molar ratio of [DCU] : [TsCl] : [TEA] was found to be 1.0 : 1.5 : 3.0. Pure DCC was obtained with a 46% yield by the sublimation after the purification process, and characterized by GC/MS, FT-IR and $^{13}C-NMR$.

• Journal of the Korean Chemical Society
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• v.56 no.5
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• pp.658-660
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• 2012

• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.40-40
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• 1993

2-Benzoyloxyacetophenones were prepared by reaction of benzooic acids and 2-hydroxyacetophenones in the presence of dicyclohexylcarbodiimide and 4-dimethylaminopyridine. The rearrangement of 2-Benzoyloxy acetophenones to 2-Dibenzoylmethans has been carried out in the presence of tetrabutylammoniumfl uoride( a phase transfer catalyst ). Both methods have been applied first for the synthesis of flavones and gave better yields of products and the reaction ran in shorter reaction time.

• Applied Chemistry for Engineering
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• v.5 no.5
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• pp.801-807
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• 1994

Lactose substituted styrene monomer, N-(p-vinylbenzyl)-D-lactonamide(VLA) was prepared by coupling the lactose lactone with p-vinylbenzylamine. The carboxyl group of biotin was activated with N-hydroxysuccinimide in the presence of N, N'-dicyclohexylcarbodiimide. Subsquently, biotin substituted styrene monomer, N-(p-vinylbenzyl)-biotinamide(VBA) was prepared by amidation of the activated biotin with p-vinylbenzylamine. Poly(vinylbenzylactonamide-co-vinylbenzylbiotinamide), p(VLA-co-VBA) were synthesized through radical polymerization from the synthetic monomers(VLA-VBA) by using various mole ratio. The percentages of yield were 67~71%. The copolymers were found amphlphilic which had hydrophilic lactose, hydrophobic vinylbenzyl and biotin site within the structure. IR and $^{13}C-NMR$ analysis on the monomers and copolymer were carried out.

• Journal of Pharmaceutical Investigation
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• v.25 no.2
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• pp.101-108
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• 1995

The surface of albumin microspheres could be modified with methotrexate (MTX) by using 1,3-dicyclohexylcarbodiimide (DCC). Surface-modified albumin microspheres entrapping no MTX (SAMS), free MTX (SAMSF) and MTX-bovine serum albumin (BSA) conjugates (SAMSC) were prepared. respectively, and their release characteristics were investigated in the presence of trypsin using a dissolution tester. The mean diameters of all the microspheres were $5{\sim}8\;{\mu}m$, and their shapes was small and uniform. MTX bound tn their surfaces was released slower than the entrapped free MTX, and laster than the entrapped MTX-BSA conjugates. Also, surface-modified MTX was scarcely released in the absence of a proteolytic enzyme. Therefore, the surface-modified MTX may be released rapidly from SAMSC at the target site, and thereafter MTX may be released slowly from the encapsulated MTX-BSA conjugates in SAMSC for a long period.

• Applied Biological Chemistry
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• v.34 no.4
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• pp.334-338
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• 1991

Synthesis of $(D-Phe^7\;-Leu^8)$ bradykinin and bradykinin by solid phase method using a new reaction vessel was carried out. Coupling was performed by dicyclohexylcarbodiimide. After cleavage with dried HBr the peptides were purified by high pressure liquied chromatography. Their purify was assayed by paper and thin layer chromatography, melting point and amino acid analysis. $(D-Phe^7\;-Leu^8)$ bradykinin and bradykinin were incubater in vitro endopeptidase $({\alpha}-chymotrysis)$ and exopeptidase(carboxypeptidase A, leucine aminopeptidase) in order to study the degradation pattern of peptides. $(D-Phe^7\;-Leu^8)$ bradykinin and bradykinin were rapidly degradated by ${\alpha}-chymotrypsin$ and carboxypeptidase A $(D-Phe^7\;-Leu^8)$ bradykinin and bradykinin coution$(D-Phe^7\;-Leu^8)$ bradykinin and bradykinin contain imino peptide bound from proline at N-terminal and therefore they were not attacted by leucine aminopeptidase.