149910-63-4Relevant academic research and scientific papers
Total and semi-syntheses of antimicrobial thuggacin derivatives
Franke, Jana,Bock, Martin,Dehn, Richard,Fohrer, J?rg,Mhaske, Santosh B.,Migliorini, Antonella,Kanakis, Argyrios A.,Jansen, Rolf,Herrmann, Jennifer,Müller, Rolf,Kirschning, Andreas
, p. 4272 - 4284 (2015)
The total and semi-synthesis of 13 new macrolactones derived from thuggacin, which is a secondary metabolite from the myxobacterium Sorangium cellulosum, are reported. The thuggacins have attracted much attention due to their strong antibacterial activity, particularly towards Mycobacterium tuberculosis. This study focuses on 1) thuggacin derivatives that cannot equilibrate by transacylation between the three natural thuggacins A-C, 2) the roles of the thiazole ring, and 3) the hexyl side chain at C2. Semi-synthetic O-methylation at C17 suppressed the transacylations without a substantial loss of antibacterial activity. Exchanging the C17-C25 side chain for simplified hydrophobic chains led to complete loss of antibacterial activity. Exchange of the thiazole by an oxazole ring or removal of the hexyl side chain at C2 had no substantial effect on the biological properties.
Stereoselective synthesis of chiral thiol-containing 1,2-aminoalcohols via SmI2-mediated coupling
Doler, Carina,Friess, Michael,Lackner, Florian,Weber, Hansj?rg,Fischer, Roland C.,Breinbauer, Rolf
, (2020/05/14)
The stereoselective synthesis of highly functionalized aminohydroxythiols represents a synthetic challenge as the oxidation sensitivity and coordinating property of the thiol group interferes with many established synthetic methods. The SmI2/Li
Improved total synthesis and biological evaluation of potent apratoxin S4 based anticancer agents with differential stability and further enhanced activity
Chen, Qi-Yin,Liu, Yanxia,Cai, Weijing,Luesch, Hendrik
, p. 3011 - 3029 (2014/05/06)
Apratoxins are cytotoxic natural products originally isolated from marine cyanobacteria that act by preventing cotranslational translocation early in the secretory pathway to downregulate receptor levels and inhibit growth factor secretion, leading to pot
Synthesis of threo-β-aminoalcohols from aminoaldehydes via chelation-controlled additions. Total synthesis of l-threo sphingosine and safingol
Jung, Michael E.,Yi, Sung Wook
supporting information; experimental part, p. 4216 - 4220 (2012/08/29)
Chelation-controlled addition of organocuprates to N-carbamoyl aminoaldehydes, prepared from functionalized amino acids, generated predominately the threo-β-amino alcohol derivatives through chelation with the carbamoyl moiety. The carbamate group is a stronger chelating group than other potentially good chelators, for example ethers, esters, thioethers, and gives good diastereoselectivity with cuprates. Thus addition of lithium divinylcuprate to the aldehyde generated from the serine derivative 25 in the presence of extra copper for chelation afforded the threo compound 26 in 83% yield. Cross-metathesis and cleavage of the protecting groups furnished l-threo sphingosine 21. In addition the lyso-sphingolipid protein kinase C inhibitor, safingol, 22, was prepared from commercially available O-benzyl N-BOC serine 28 in six steps and 56% overall yield by this method.
Convergent synthesis of peptide nucleic acids by native chemical ligation
Dose, Christian,Seitz, Oliver
, p. 4365 - 4368 (2007/10/03)
(Chemical Equation Presented) A convergent strategy for synthesizing long contiguous PNA by a native chemical ligation-like technique of PNA segment couplings is presented. This approach required the synthesis of a new PNA-monomer featuring a 1-amino-2-th
Prenyl transferase inhibitors
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, (2008/06/13)
A family of compounds capable of inhibiting the activity of prenyl transferases. The compounds are covered by the four following formulas Each of the R groups is defined in the disclosure.
Prenyl transferase inhibitors
-
, (2008/06/13)
A family of compounds capable of inhibiting the activity of prenyl transferases. The compounds are covered by either of the two following formulas STR1 Each of the R groups is defined in the disclosure.
INHIBITORS OF FARNESYL-PROTEIN TRANSFERASE
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, (2008/06/13)
The present invention comprises dipeptide analogs that inhibit the farnesylation of Ras. These farnesyl-protein transferase inhibitors are characterized by the inclusion of a cyclic amine in the backbone of the dipeptide. Further contained in this inventi
Design and synthesis of non-peptide Ras CAAX mimetics as potent farnesyltransferase inhibitors
Qian, Yimin,Vogt, Andreas,Sebti, Sa?d M.,Hamilton, Andrew D.
, p. 217 - 223 (2007/10/03)
Cysteine farnesylation of the ras oncogene product Ras is required for its transforming activity and is catalyzed by farnesyltransferase (FTase). The Ras carboxyl terminal tetrapeptide CAAX (C is cysteine, A is any aliphatic amino acid, X is methionine or serine) is the minimum sequence for FTase recognition. We report here the design, synthesis, and biological characterization of Ras CAAX non-peptide mimetics in which the cysteine is linked through a reduced pseudopeptide bond to 4-amino-3'-carboxybiphenyl. These non-peptide mimetics are potent inhibitors of FTase (IC50 = 40 nM for the most potent inhibitor) and are highly selective for FTase over GGTase I (geranylgeranyltransferase I). They are not substrates for farnesylation, do not have peptidic features, and have no hydrolyzable bonds. Structure- activity studies reveal the importance of the position of the carboxylic acid on the aryl ring as well as the reduction of the cysteine amide bond. Substitution at the 2-position of 4-amino-3'-carboxybiphenyl increases inhibitory potency, while the removal of the carboxylic acid results in a 10- fold loss of inhibitory activity.
Inhibitors of farnesyl-protein transferase
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, (2008/06/13)
The present invention is directed to compounds which inhibit farnesyl-protein transferase (FTase) and the farnesylation of the oncogene protein Ras. The invention is further directed to chemotherapeutic compositions containing the compounds of this invent
