- Amino Acid Functionalized Organotin Trichlorides and Their Tin Sulfide Clusters
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We present a new synthesis of functionalized tin sulfide clusters via organotin trichlorides with boc-protected amino acids (RAAcSnCl3). In this work we used non-polar (alanine, valine, leucine, phenylalanine and methionine), polar/neutral (serine and tyrosine) and basic (histidine) amino acids. We obtained single crystals from a Boc-protected valine derivative of the originally used organotin trichloride R1SnCl3 [R1 = CMe2CH2C(O)Me] and determined its structure by means of X-ray diffraction. A subsequent reaction with sulfide sources led to a variety of respective cluster structures. By using either (Me3Si)2S or Na2S, the reaction product turns out to be the defect-heterocubane cluster [(RAAcSn)3S4Cl] or the “doppeldecker”-type cluster [(RAAcSn)4S6], respectively, according to 119Sn NMR spectroscopy.
- Engel, Annikka,Dehnen, Stefanie
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- Synthesis of 5 H -Pyrrolo[3,4- b ]pyrazine-Based Peptidomimetics
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A range of 5H-pyrrolo[3,4-b]pyrazine-based peptidomimetics were designed, and their efficient synthesis starting from 5-imino-5H-pyrrolo[3,4-b]pyrazin-7-amine by subsequent interaction with N-protected amino acid hydrazides and amino acid esters with N,N-carbonyldiimidazole as the coupling agent was elaborated.
- Biitseva, Angelina V.,Rudenko, Igor V.,Hordiyenko, Olga V.,Omelchenko, Iryna V.,Arrault, Axelle
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p. 3733 - 3740
(2015/11/28)
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- Design, synthesis and biological evaluation of a library of thiocarbazates and their activity as cysteine protease inhibitors
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Recently, we identified a novel class of potent cathepsin L inhibitors, characterized by a thiocarbazate warhead. Given the potential of these compounds to inhibit other cysteine proteases, we designed and synthesized a library of thiocarbazates containing diversity elements at three positions. Biological characterization of this library for activity against a panel of proteases indicated a significant preference for members of the papain family of cysteine proteases over serine, metallo-, and certain classes of cysteine proteases, such as caspases. Several potent inhibitors of cathepsin L and S were identified. The SAR data were employed in docking studies in an effort to understand the structural elements required for cathepsin S inhibition. This study provides the basis for the design of highly potent and selective inhibitors of the papain family of cysteine proteases.
- Liu, Zhuqing,Myers, Michael C.,Shah, Parag P.,Beavers, Mary Pat,Benedetti, Phillip A.,Diamond, Scott L.,Smith, Amos B.,Huryn, Donna M.
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experimental part
p. 337 - 351
(2010/09/04)
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