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Allyltrichlorostannane additions to alpha-amino aldehydes: Application to the total synthesis of the aspartyl protease inhibitors L-682,679, L-684,414, L-685,434, and L-685,458
(Georg Thieme Verlag KgStuttgartAlemanha, 2003)
Novel and facile solution-phase synthesis of 2,5-diketopiperazines and O-glycosylated analogs
(PERGAMON-ELSEVIER SCIENCE LTD, 2009)
This work describes the synthesis in Solution of a series of related diketopiperazines with potential biological activities: cyclo(L-Pro-L-Ser), cyclo(L-Phe-L-Ser), cyclo(D-Phe-L-Ser) and the corresponding glycosylated ...
Polymer-Supported Stereoselective Synthesis of Tetrahydro-2H-oxazolo[3,2-a]pyrazin-5(3H)-ones from N-(2-Oxo-ethyl)-Derivatized Dipeptides via Eastbound Iminiums
(American Chemical Society, 2013-02)
Polymer-supported N-(2-oxo-ethyl)-derivatized Ser/Thr/Cys-containing dipeptides were synthesized and subjected to acid-mediated tandem N-acylium ion cyclization−nucleophilic addition to yield tetrahydro-2H-oxazolo- ...
Understanding The Conformational Behaviour Of Ac-ala-nhme In Different Media. A Joint Nmr And Dft Study
(ROYAL SOC CHEMISTRYCAMBRIDGE, 2015)
Addition of allyltrichlorostannanes to aldehydes: application in the synthesis of 4-N-Boc-amino-3-hydroxy ketones
(Pergamon-elsevier Science LtdOxfordInglaterra, 2008)
The Baylis-Hillman reaction with chiral alpha-amino aldehydes under racemization-free conditions
(Georg Thieme Verlag KgStuttgartAlemanha, 2006)
Diketopiperazines produced by an Aspergillus fumigatus Brazilian strain
(Soc Brasileira QuimicaSao PauloBrasil, 2005)
Short total synthesis of aspartyl protease inhibitors L-685,434, L-682,679 and L-685,458
(Georg Thieme Verlag KgStuttgartAlemanha, 2002)
Interaction of Cu-dipeptide complexes with Calf Thymus DNA and antiproliferative activity of [Cu(ala-phe)] in osteosarcoma-derived cells
(Pergamon-Elsevier ScienceOxford, 2009-08)
In this work the study of Calf Thymus DNA interaction with several Cu(l-dipeptide) complexes was reported. The binding stoichiometry (Cu(mmol)/DNAmol base) was determined and in an attempt to clarify the binding mode, EPR ...
FUNCTIONAL ALPHA-TROPOMYOSIN PRODUCED IN ESCHERICHIA-COLI - A DIPEPTIDE EXTENSION CAN SUBSTITUTE THE AMINO-TERMINAL ACETYL GROUP
(Amer Soc Biochemistry Molecular Biology Inc, 1994-04-08)
Unlike the muscle protein, alpha-tropomyosin expressed in Escherichia coli does not bind actin, does not exhibit head-to-tail polymerization, and does not inhibit actomyosin ATPase activity in the absence of troponin. The ...