75768-66-0Relevant articles and documents
Aminoacid-derivatized Cu (II) complexes: Synthesis, DNA interactions and in vitro cytotoxicity
Singh, Rinky,Devi, P. Rama,Jana, Sharmita S.,Devkar, Ranjitsinh V.,Chakraborty, Debjani
, p. 157 - 169 (2017/09/30)
Two different series of copper complexes, [Cu(MFL)(FcAA)H2O] (C1-C4) and [Cu(MFL) (BzAA)H2O] (C5-C8), where FcAA = ferrocenyl amino acid mannich base conjugates and BzAA = benzaldehyde amino acid mannich base conjugates have been syn
Structure-Activity Relationships of the Peptide Kappa Opioid Receptor Antagonist Zyklophin
Joshi, Anand A.,Murray, Thomas F.,Aldrich, Jane V.
, p. 8783 - 8795 (2015/12/08)
The dynorphin (Dyn) A analogue zyklophin ([N-benzyl-Tyr1-cyclo(d-Asp5,Dap8)]dynorphin A(1-11)NH2) is a kappa opioid receptor (KOR)-selective antagonist in vitro, is active in vivo, and antagonizes KOR in the CNS
Controlling the self-assembly of homochiral coordination architectures of CuII by substitution in amino acid based ligands: Synthesis, crystal structures and physicochemical properties
Kumar, Navnita,Khullar, Sadhika,Mandal, Sanjay K.
, p. 5672 - 5687 (2015/03/30)
Through the strategic design of ligands based on amino acids, structural diversity in chiral coordination architectures of CuII is demonstrated with six new examples: {[Cu(l-HTyrbenz)2]·CH3OH·H2O}n (1), {[Cu(l-HSerbenz)2]·3H2O}n (2), {[Cu(l-HTyrthio)2]·H2O}n (3), [Cu(l-HTyr4-pyr)2(H2O)]·2H2O (4), [Cu(l-HSerthio)2(H2O)] (5), and [Cu(l-Phethio)2(H2O)]·3H2O (6) [where l-H2Tyrbenz = l-N-(benzyl)-tyrosine, l-H2Serbenz = l-N-(benzyl)-serine, l-H2Tyrthio = l-N-(methyl-2-thiophenyl)-tyrosine, l-H2Tyr4-pyr = l-N-(methyl-4-pyridyl)-tyrosine, l-H2Serthio = l-N-(methyl-2-thiophenyl)-serine and l-HPhethio = l-N-(methyl-2-thiophenyl)-phenylalanine]. For these 1:2 metal-ligand complexes, the availability of a donor atom (either from the phenolic OH group or the carboxylate group of one of the ligands) for bridging between the CuII centers results in the formation of coordination polymers (1-3), while no such availability allows a water molecule to occupy the fifth site around the CuII center to generate hydrogen bonded supramolecular assemblies (4-6). In 1, a coordination polymer is formed via a syn-anti bridging carboxylate, and the phenolic group has no role in its formation. To further emphasize this point, l-tyrosine in 1 is replaced with l-serine to form 2, in which an anti-anti bridging by the carboxylate group is observed. On the other hand, the formation of {[Cu(l-HTyrthio)2]·H2O}n (3) results from the growth of a spiral polymer via the unique phenolic bridging with a distance of 10.806(9) ? between two CuII centers. On changing from the l-H2Tyrbenz ligand to the l-H2Tyr4-pyr ligand (1vs.4), the strong hydrogen bonding of the pyridyl nitrogen with the phenolic group does not allow the latter to bind to CuII. Similarly, on changing from l-H2Tyrthio to l-H2Serthio (3vs.5), the length of the -CH2OH group in the latter is much less than the distance between the two CuII centers, therefore this group cannot occupy the fifth site and thus a water molecule is coordinated. This is further confirmed by reacting 5 with 2 eq. of l-H2Tyrthio in methanol to form 3, while the reverse is not possible. All these compounds are characterized by a number of analytical methods, such as elemental analysis, FTIR, UV-Vis and circular dichroism spectroscopy, polarimetry, powder and single crystal X-ray diffraction and thermogravimetric analysis. Photoluminescence properties of all ligands containing the l-tyrosine group and their metal complexes (1, 3 and 4) are compared in solution at room temperature. This journal is
Photocytotoxic ferrocene-appended (l-tyrosine)copper(II) complexes of phenanthroline bases
Goswami, Tridib K.,Gadadhar, Sudarshan,Karande, Anjali A.,Chakravarty, Akhil R.
, p. 1287 - 1298 (2013/07/11)
Copper(II) complexes of ferrocene(Fc)-conjugated reduced Schiff base of l-tyrosine (Fc-TyrH), viz., [Cu(Fc-Tyr)(L)](ClO4), where L is 1,10-phenanthroline (phen, 1), dipyrido[3,2-d:2′,3′-f]quinoxaline (dpq, 2), dipyrido[3,2-a:2′,3′-c]phenazine (
The effects of C-terminal modifications on the opioid activity of [N-benzylTyr1]dynorphin A-(1-11) analogues
Patkar, Kshitij A.,Murray, Thomas F.,Aldrich, Jane V.
supporting information; experimental part, p. 6814 - 6821 (2010/03/31)
Structural modifications affecting the efficacy of analogues of the endogenous opioid peptide dynorphin (Dyn) A have focused on the N-terminal "message" sequence based on the "message-address" concept. To test the hypothesis that changes in the C-terminal
Cyanopeptolin 954, a chlorine-containing chymotrypsin inhibitor of Microcystis aeruginosa NIVA Cya 43
Von Elert, Eric,Oberer, Lukas,Merkel, Petra,Huhn, Thomas,Blom, Judith F.
, p. 1324 - 1327 (2008/09/17)
A new depsipeptide, cyanopeptolin 954 (1), was isolated from the freshwater cyanobacterium Microcystis aeruginosa NIVA Cya 43. The structure of the compound was elucidated by chemical and spectroscopic analyses, including 2D NMR and GC-MS of the hydrolysate. The major structural differences compared to previously characterized heptadepsipeptides of Microcystis are the replacement of the basic amino acid in position 4 by L-leucine, the presence of L-phenylalanine in position 6, and the uncommon residue 3′-chloro-N-Me-L- tyrosine in position 7. Cyanopeptolin 954 inhibited chymotrypsin with an IC 50 value of 45 nM. Nostopeptin BN920, formerly isolated from the cyanobacterium Nostoc, was isolated from the same strain of Microcystis, and a cis amide bond between Phe (6) and N-Me-Tyr (7) was shown. Nostopeptin BN920 inhibited chymotrypsin with an IC50 value of 31 nM.
Sodium borohydride: A versatile reagent in the reductive N-monoalkylation of α-amino acids and α-amino methyl esters
Verardo, Giancarlo,Geatti, Paola,Pol, Elena,Giumanini, Angelo G.
, p. 779 - 788 (2007/10/03)
α-Amino acids and α-amino methyl esters are easily converted to their N-monoalkyl derivatives by a reductive condensation reaction using several carbonyl compounds in the presence of sodium borohydride. This reducing agent has shown a wide versatility with minor but essential procedural variations. The reaction allows the α-monodeuterium labeling of the new N-substituent by use of sodium borodeuteride.
Synthesis and opioid activity of [D-Pro10]Dynorphin A-(1-11) analogues with N-terminal alkyl substitution
Choi, Heekyung,Murray, Thomas F.,DeLander, Gary E.,Schmidt, William K.,Aldrich, Jane V.
, p. 2733 - 2739 (2007/10/03)
Several N-terminal di- and monoalkylated derivatives of [D- Pro10]dynorphin A-(1-11) were synthesized in order to explore the structure-activity relationships for antagonist vs agonist activity at κ- opioid receptors. N,N-Dialkylated and N-monoalkylated (alkyl = allyl, benzyl, and cyclopropylmethyl (CPM)) tyrosine derivatives were prepared from tyrosine tert-butyl ester and the corresponding alkyl halides. [D-Pro10]Dyn A-(2- 11) was prepared by solid phase synthesis using Fmoc-protected amino acids, and the tyrosine derivatives were coupled to the peptide with BOP ((benzotriazol-1-yloxy)tris(dimethylamino)phosphonium hexafluorophosphate). Both the degree of substitution and the identity of the alkyl group affected κ-receptor affinity, selectivity, and efficacy. All of the N-monoalkylated derivatives exhibited much higher affinity (K(i) 200) compared to the N,N-dialkyl [D-Pro10]Dyn A-(1- 11) analogues, although one disubstituted analogue, N,N-diCPM[D-Pro10]Dyn A-(1-11), retained high affinity (K(i) = 0.19 nM) for κ receptors. Thus the introduction of the second alkyl group at the N-terminus lowered κ-receptor affinity and selectivity. The N-allyl and N-CPM analogues were moderately potent agonists in the guinea pig ileum (GPI) assay, while the N-benzyl derivative was a weak agonist in this assay. In vivo in the phenylqninone abdominal stretching assay the N-CPM analogue exhibited potent antinociceptive activity (ED50 = 1.1 μg/mouse), while N-allyl[D- Pro10]Dyn A-(l-11) exhibited weak antinociceptive activity (ED50 = 27 μg/mouse). For the N,N-dialkyl derivatives the identity of the N-terminal alkyl group affected the efficacy observed in the smooth muscle assays. The N,N-diCPM analogue exhibited negligible agonist activity, and N,N-diallyl[D- Pro10]Dyn A-(l-11) showed weak antagonist activity against Dyn A-(1- 13)NH2 in the GPI. In contrast, the N,N-dibenzyl compound showed appreciable opioid agonist activity in this assay. In vivo the N,N-diallyl analogue exhibited weak antinociceptive activity (ED50 = 26 μg/mouse in the phenylquinone abdominal stretching assay). The N-monoalkylated peptides are among the most κ-selective opioid peptides reported to date, showing comparable or greater selectivity and higher affinity than the κ-selective nonpeptide agonists U-50,488 and U-69,593. The N,N-diCPM and N,N-diallyl peptides are lead compounds in the development of peptide-based κ-receptor antagonists.
