329318-60-7Relevant academic research and scientific papers
Aromatic Foldamer Helices as α-Helix Extended Surface Mimetics
Csékei, Márton,Fischer, Lucile,Huc, Ivan,Kotschy, András,Mandal, Pradeep K.,Reddy, Post Sai,Wicher, Barbara,Zwillinger, Márton
supporting information, p. 17366 - 17370 (2020/12/02)
Helically folded aromatic oligoamide foldamers have a size and geometrical parameters very distinct from those of α-helices and are not obvious candidates for α-helix mimicry. Nevertheless, they offer multiple sites for attaching side chains. It was found that some arrays of side chains at the surface of an aromatic helix make it possible to mimic extended α-helical surfaces. Synthetic methods were developed to produce quinoline monomers suitably functionalized for solid phase synthesis. A dodecamer was prepared. Its crystal structure validated the initial design and showed helix bundling involving the α-helix-like interface. These results open up new uses of aromatic helices to recognize protein surfaces and to program helix bundling in water.
Reagents for the quantitation of active oxygen
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, (2008/06/13)
A compound represented by general formula (I) or (II) or a salt thereof and an agent for measurement of a reactive oxygen comprising said compound or a salt thereof: 1wherein R1 and R2 independently represent an aryl group which may
Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding
Davidson, James P.,Lubman, Olga,Rose, Thierry,Waksman, Gabriel,Martin, Stephen F.
, p. 205 - 215 (2007/10/03)
Isothermal titration calorimetry and X-ray crystallography have been used to determine the structural and thermodynamic consequences associated with constraining the pTyr residue of the pYEEI ligand for the Src Homology 2 domain of the Src kinase (Src SH2
Use of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide mimics in SH2 antagonists
Davidson,Martin
, p. 9459 - 9464 (2007/10/03)
Novel conformationally constrained phosphotyrosine pseudopeptide derivatives of the tetrapeptide pY-E-E-I were prepared and evaluated as SH2 binding antagonists. (C) 2000 Elsevier Science Ltd.
