A New Method for Selective Protection of Two Hydroxyl Groups in Carbohydorates, Glycals in Particular

Heterocycles ◽  
1991 ◽  
Vol 32 (8) ◽  
pp. 1445 ◽  
Author(s):  
Cedric W. Holzapfel ◽  
Johan J. Huyser ◽  
Thilo L. van der Merwe ◽  
Fanie R. van Heerden
ChemInform ◽  
2010 ◽  
Vol 23 (4) ◽  
pp. no-no
Author(s):  
C. W. HOLZAPFEL ◽  
J. J. HUYSER ◽  
T. L. VAN DER MERWE ◽  
F. R. VAN HEERDEN

1994 ◽  
Vol 59 (2) ◽  
pp. 457-460 ◽  
Author(s):  
Ladislav Kohout
Keyword(s):  

Brassinosteroids with lactone B-ring (II and IV) were prepared by oxidation of the corresponding 6-keto derivatives I and III without protection of the hydroxyl groups against the action of the oxidation reagent.


2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Sira Defaus ◽  
Maria Gallo ◽  
María A. Abengózar ◽  
Luis Rivas ◽  
David Andreu

A successful approach to deliver paromomycin, a poorly absorbed aminoglycoside antibiotic, to parasite cells is reported, based on selective protection of amino and hydroxyl groups followed by conjugation to a fluorolabeled, PEG-functionalized cell-penetrating Tat(48-60) peptide. The resulting construct is efficiently internalized into Leishmania cells, evidencing the fitness of cell-penetrating peptides as vectors for efficiently transporting low-bioavailability drugs into cells.


Author(s):  
Nian-Guang Li ◽  
Zhi-Hao Shi ◽  
Yu-Ping Tang ◽  
Jian-Ping Yang ◽  
Jin-Ao Duan

An efficient partial 5-step synthesis of 4′-O-methylquercetin from quercetin in 63% yield is reported. This strategy relies on the selective protection of the catechol group with dichlorodiphenylmethane in diphenyl ether as solvent and on the selective protection of the hydroxyl groups at positions 3 and 7 with chloromethyl ether.


ChemInform ◽  
2010 ◽  
Vol 29 (30) ◽  
pp. no-no
Author(s):  
R. A. HOLTON ◽  
Z. ZHANG ◽  
P. A. CLARKE ◽  
H. NADIZADEH ◽  
D. J. PROCTER

2013 ◽  
Vol 6 (1) ◽  
pp. 115-122 ◽  
Author(s):  
Martina Danihelová ◽  
Miroslav Veverka ◽  
Ernest Šturdík

Abstract Novel quercetin derivatives were prepared to change its physicochemical properties and effects on activity of proteolytic enzymes. For them preparation, the selective protection procedures some of the quercetin hydroxyl groups and acylation of the others with acylchlorides were used. The ability of these compounds to inhibit the activity of serine proteases e.g. trypsin, thrombin, urokinase and elastase was studied. In micromolar range, tested derivatives were the most potent inhibitors of thrombin. There was estimated better inhibition of thrombin for prenylated, acetylated, feruloyl and caffeoyl quercetin esters. Slight inhibitory effect of all quercetin derivatives on elastase was found. Among tested derivatives only diquercetin displayed better inhibiton. Trypsin and urokinase were inhibited by quercetin at comparable level. Slight improvement in inhibitory effect of trypsin and urokinase was seen for chloronaphtoquinone quercetin that revealed enhanced inhibiton of thrombin, too. However, no influence on elastase activity was determined for this compound. Obtained results indicate that certain modifications of quercetin structure could improve its biological properties.


1974 ◽  
Vol 5 (48) ◽  
pp. no-no
Author(s):  
K. K. OGILVIE ◽  
E. A. THOMPSON ◽  
M. A. QUILLIAM ◽  
J. B. WESTMORE

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