122235-70-5Relevant articles and documents
Fluorophore ATCUN complexes: Combining agent and probe for oxidative DNA cleavage
Wende,Kulak
, p. 12395 - 12398 (2015)
DNA can be oxidatively cleaved by copper complexes of the ATCUN peptide (amino terminal Cu(II)- and Ni(II)-binding motif). In order to investigate the fate of the metal ion throughout this process, we have exploited quenching/dequenching effects of conjugated fluorophores.
2,3-Diaminopropanols obtained from D-serine as intermediates in the synthesis of protected 2,3-L-diaminopropanoic acid (L-DAP) methyl esters
Aiello, Donatella,Athanassopoulos, Constantinos M.,Mazzotti, Fabio,Siciliano, Carlo,Temperini, Andrea,de Luca, Pierantonio
, (2020/03/23)
A synthetic strategy for the preparation of two orthogonally protected methyl esters of the non-proteinogenic amino acid 2,3-l-diaminopropanoic acid (l-Dap) was developed. In these structures, the base-labile protecting group 9-fluorenylmethyloxycarbonyl (Fmoc) was paired to the p-toluensulfonyl (tosyl, Ts) or acid-labile tert-butyloxycarbonyl (Boc) moieties. The synthetic approach to protected l-Dap methyl esters uses appropriately masked 2,3-diaminopropanols, which are obtained via reductive amination of an aldehyde prepared from the commercial amino acid Nα-Fmoc-O-tert-butyl-d-serine, used as the starting material. Reductive amination is carried out with primary amines and sulfonamides, and the process is assisted by the Lewis acid Ti(OiPr)4. The required carboxyl group is installed by oxidizing the alcoholic function of 2,3-diaminopropanols bearing the tosyl or benzyl protecting group on the 3-NH2 site. The procedure can easily be applied using the crude product obtained after each step, minimizing the need for chromatographic purifications. Chirality of the carbon atom of the starting d-serine template is preserved throughout all synthetic steps.
COMPOUNDS AND USES THEREOF
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Page/Page column 123-124, (2019/08/26)
The present disclosure features compounds useful for the treatment of BAF complex-related disorders.
Iridium-catalyzed asymmetric allylic amination with polar amines: Access to building blocks with lead-like molecular properties
Tosatti, Paolo,Horn, Joachim,Campbell, Amanda J.,House, David,Nelson, Adam,Marsden, Stephen P.
supporting information; experimental part, p. 3153 - 3157 (2011/03/18)
The combination of an air-stable iridium catalyst and the dipolar aprotic solvent dimethyl sulfoxide (DMSO) allowed, for the first time, the systematic exploitation of highly polar, functionalized amines in asymmetric allylic substitutions: low molecular
Diaminopropionic acid derivatives
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, (2008/06/13)
A compound of formula 1a which is useful for treating reperfusion injury, and salts, prodrugs, and related compounds.
Synthesis and study of peptides with semirigid i and i+7 side-chain bridges designed for α-helix stabilization
Yu, Chongxi,Taylor, John W.
, p. 161 - 175 (2007/10/03)
A search for conformational constraints on the peptide α-helical conformation indicated that para-substituted amino acid derivatives of a benzene ring might be suitable for linking pairs of side chains that are separated by two turns of the helix. A 14-residue synthetic, amphiphilic α-helical peptide model system has been used to study the helix stabilizing effects of a series of four such bridges having constitutionally isomeric structures. These bridges were used to link positions 3 and 10 of the model peptides. The peptides were synthesized in good yield by standard solid-phase methods, including cyclization on the solid support. They were then studied for their solution conformations and melting behavior by circular dichroism (CD) spectropolarimetry, and for their elution behavior on reversed-phase HPLC columns. In aqueous solution and in 50% (v/v) trifluoroethanol, the most effective bridge for helix stabilization consisted of a 4-(aminomethyl)phenylacetic acid residue (AMPA) linked by amide bonds to the side chain functional groups of a (S)-2,3-diaminopropionic acid residue (Dap) in position 3 of the model peptide and an aspartic acid residue in position 10. This Dap3(AMPA), Asp10 bridge was about as effective as two Lys(i), Asp(i+4) lactam bridges incorporated linking residues 3 and 7, and 10 and 14, in the same model peptide sequence. This suggests that it is worth about 1kcal/mol of helix stabilization energy. Copyright (C) 1999 Elsevier Science Ltd.
Synthesis of Peptides Containing Unnatural, Metal-Ligating Residues: Aminodiacetic Acid as a Peptide Side Chain
Ruan, Fuqiang,Chen, Yanqiu,Itoh, Katsumi,Sasaki, Tomikazu,Hopkins, Paul B.
, p. 4347 - 4354 (2007/10/02)
Peptides possessing a pair of residues separated by one turn in the α-helical conformation and potentially capable of ligating a single metal ion in aqueous solution were designed.It was predicted that the resulting cross-link would shift toward α-helix the random coil/α-helix equilibrium.The syntheses of 10 peptides Ac-AdalAlamAdal(Ala4GluLys)n-NH2 where Adal is an L-α-amino acid residue with an aminodiacetic acid bearing side chain, -(CH2)lN(CH2CO2H)2 (with values of l, m and n as follows: 1, 2, 3 (1); 1, 3, 1 (2a); 1, 3, 2 (2b); 1, 3, 3 (2c); 2, 2, 3 (3); 2, 3, 3 (4); 3, 2 ,3 (5); 3, 3, 3 (6); 4, 2, 3 (7); 4, 3, 3 (8) are described using Boc chemistry on p-methylbenzhydrylamine resin.The aminodiacetic acid bearing residues were incorporated with side chains protected as the dibenzyl esters.To avoid side reactions, residues Adal for l=1 and 2 were incorporated by a block approach.Peptide structures were confirmed by observation of the predicted parent ions in the FAB MS.The circular dichroism spectra of several of these peptides that possess a pair of metal-ligating residues separated by two or three intervening residues have previously been shown to undergo changes on addition of metal ions consistent with appreciable enhancement of helix content.
Potent and Prolonged Acting Cyclic Lactam Analogues of α-Melanotropin: Design Based on Molecular Dynamics
Al-Obeidi, Fahad,Castrucci, Ana M. de L.,Hadley, Mac E.,Hruby, Victor J.
, p. 2555 - 2561 (2007/10/02)
Utilizing results from previous structure-activity relationships and theoretical studies of α-melanotropin (α-MSH, Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2) and its related superpotent analogues, Ac-4,D-Phe7>-α-MSH and , we have designed a new class of α-MSH4-13 and α-MSH4-10 cyclic lactam fragment analogues of α-melanotropin.The cyclic peptides have the following general structures: and , where Xxx = Glu or Asp and Yyy = Lys, Orn, Dab, or Dpr.Formation of the lactam bridge between the side-chain groups Xxx and Yyy was performed either in solution or on a solid-phase support.Seven cyclic peptides were prepared and bioassayed for their melanotropic potency by using standard frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays.Relative to α-MSH (relative potency = 1), the potencies of the cyclic peptides in the lizard skin bioassay were as follows: α-MSH (1); (6); (100); (9); (90), (20); (5); (5).Similar results were obtained in the frog skin bioassay, but the analogues were much less potent.Cyclic melanotropins with 23-membered rings exhibited 100-fold higher melanotropic potency than α-MSH with selectivity for the lizard melanocyte receptors over the frog melanocyte receptors.Increasing or decreasing the ring size of these cyclic melanotropins from 23 diminishes the biological potency of the resulting cyclic peptide.The 23- and 24-membered ring analogues showed prologed (residual) biological activities in both biological assays, but the smaller ring systems (20, 21, 22) did not.These results provide new insights into the structural and conformational requirements of α-MSH and its analogues at two different types of pigment cell (melanocyte) receptors.
