The Experts below are selected from a list of 19782 Experts worldwide ranked by ideXlab platform
Pascale Delangle - One of the best experts on this subject based on the ideXlab platform.
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Pseudo-peptides Based on Methyl Cysteine or Methionine Inspired from Mets Motifs Found in the Copper Transporter Ctr1
Inorganic Chemistry, 2015Co-Authors: Anne-solene Jullien, Christelle Gateau, Colette Lebrun, Pascale DelangleAbstract:Most proteins involved in Cu homeostasis bind to intracellular Cu(I) in stable Cu(S-Cys)(x) environments, thanks to well-conserved cysteine-rich sequences. Similarly, the Cu(I) transport protein Ctr1, responsible for copper acquisition, binds Cu(I) in Cu(S-Met)(3) environments in conserved methionine-rich MXMXXM sequences, referred as Mets motifs. Pseudo-peptides based on a nitrilotriacetic acid scaffold and functionalized with three amino acids bearing thioether side chains, either methyl cysteine in T-1 or methionine in T-2, were synthesized as mimics of the Mets sequences found in Ctr1. These two ligands were obtained with good overall yields from commercial amino acids and demonstrate efficient chelating ability for Cu(I). Only one species, the mononuclear [CuT1,2](+) complex, was evidenced by electrospray ionizationmass spectroscopy (ESI-MS) and the circular dichroism signature obtained for the most constrained CuT1 complex having the shortest side chains showed reorganization of the pseudo-peptide scaffold upon Cu(I) complexation. Considering that thioether functions are neutral sulfur donors, the stability constants measured by competition with ferrozine are quite large: log K approximate to 10.2-10.3. The CuT1,(2) complexes are significantly more stable that those formed with linear peptides, mimicking isolated Mets motifs MXMXXM of the Cu transport protein Ctr1 (log K approximate to 5-6). This may be attributed to the preorganized pseudo-peptide scaffold, which arranges the three neutral sulfur donors toward the metal center. Such moderate affinity Cu(I) chelators are interesting for applications in chelation therapy, for instance, to induce minimum disturbance of Cu homeostasis in Wilsons Disease treatments.
Anne-solene Jullien - One of the best experts on this subject based on the ideXlab platform.
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Pseudo-peptides Based on Methyl Cysteine or Methionine Inspired from Mets Motifs Found in the Copper Transporter Ctr1
Inorganic Chemistry, 2015Co-Authors: Anne-solene Jullien, Christelle Gateau, Colette Lebrun, Pascale DelangleAbstract:Most proteins involved in Cu homeostasis bind to intracellular Cu(I) in stable Cu(S-Cys)(x) environments, thanks to well-conserved cysteine-rich sequences. Similarly, the Cu(I) transport protein Ctr1, responsible for copper acquisition, binds Cu(I) in Cu(S-Met)(3) environments in conserved methionine-rich MXMXXM sequences, referred as Mets motifs. Pseudo-peptides based on a nitrilotriacetic acid scaffold and functionalized with three amino acids bearing thioether side chains, either methyl cysteine in T-1 or methionine in T-2, were synthesized as mimics of the Mets sequences found in Ctr1. These two ligands were obtained with good overall yields from commercial amino acids and demonstrate efficient chelating ability for Cu(I). Only one species, the mononuclear [CuT1,2](+) complex, was evidenced by electrospray ionizationmass spectroscopy (ESI-MS) and the circular dichroism signature obtained for the most constrained CuT1 complex having the shortest side chains showed reorganization of the pseudo-peptide scaffold upon Cu(I) complexation. Considering that thioether functions are neutral sulfur donors, the stability constants measured by competition with ferrozine are quite large: log K approximate to 10.2-10.3. The CuT1,(2) complexes are significantly more stable that those formed with linear peptides, mimicking isolated Mets motifs MXMXXM of the Cu transport protein Ctr1 (log K approximate to 5-6). This may be attributed to the preorganized pseudo-peptide scaffold, which arranges the three neutral sulfur donors toward the metal center. Such moderate affinity Cu(I) chelators are interesting for applications in chelation therapy, for instance, to induce minimum disturbance of Cu homeostasis in Wilsons Disease treatments.
Christelle Gateau - One of the best experts on this subject based on the ideXlab platform.
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Pseudo-peptides Based on Methyl Cysteine or Methionine Inspired from Mets Motifs Found in the Copper Transporter Ctr1
Inorganic Chemistry, 2015Co-Authors: Anne-solene Jullien, Christelle Gateau, Colette Lebrun, Pascale DelangleAbstract:Most proteins involved in Cu homeostasis bind to intracellular Cu(I) in stable Cu(S-Cys)(x) environments, thanks to well-conserved cysteine-rich sequences. Similarly, the Cu(I) transport protein Ctr1, responsible for copper acquisition, binds Cu(I) in Cu(S-Met)(3) environments in conserved methionine-rich MXMXXM sequences, referred as Mets motifs. Pseudo-peptides based on a nitrilotriacetic acid scaffold and functionalized with three amino acids bearing thioether side chains, either methyl cysteine in T-1 or methionine in T-2, were synthesized as mimics of the Mets sequences found in Ctr1. These two ligands were obtained with good overall yields from commercial amino acids and demonstrate efficient chelating ability for Cu(I). Only one species, the mononuclear [CuT1,2](+) complex, was evidenced by electrospray ionizationmass spectroscopy (ESI-MS) and the circular dichroism signature obtained for the most constrained CuT1 complex having the shortest side chains showed reorganization of the pseudo-peptide scaffold upon Cu(I) complexation. Considering that thioether functions are neutral sulfur donors, the stability constants measured by competition with ferrozine are quite large: log K approximate to 10.2-10.3. The CuT1,(2) complexes are significantly more stable that those formed with linear peptides, mimicking isolated Mets motifs MXMXXM of the Cu transport protein Ctr1 (log K approximate to 5-6). This may be attributed to the preorganized pseudo-peptide scaffold, which arranges the three neutral sulfur donors toward the metal center. Such moderate affinity Cu(I) chelators are interesting for applications in chelation therapy, for instance, to induce minimum disturbance of Cu homeostasis in Wilsons Disease treatments.
Colette Lebrun - One of the best experts on this subject based on the ideXlab platform.
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Pseudo-peptides Based on Methyl Cysteine or Methionine Inspired from Mets Motifs Found in the Copper Transporter Ctr1
Inorganic Chemistry, 2015Co-Authors: Anne-solene Jullien, Christelle Gateau, Colette Lebrun, Pascale DelangleAbstract:Most proteins involved in Cu homeostasis bind to intracellular Cu(I) in stable Cu(S-Cys)(x) environments, thanks to well-conserved cysteine-rich sequences. Similarly, the Cu(I) transport protein Ctr1, responsible for copper acquisition, binds Cu(I) in Cu(S-Met)(3) environments in conserved methionine-rich MXMXXM sequences, referred as Mets motifs. Pseudo-peptides based on a nitrilotriacetic acid scaffold and functionalized with three amino acids bearing thioether side chains, either methyl cysteine in T-1 or methionine in T-2, were synthesized as mimics of the Mets sequences found in Ctr1. These two ligands were obtained with good overall yields from commercial amino acids and demonstrate efficient chelating ability for Cu(I). Only one species, the mononuclear [CuT1,2](+) complex, was evidenced by electrospray ionizationmass spectroscopy (ESI-MS) and the circular dichroism signature obtained for the most constrained CuT1 complex having the shortest side chains showed reorganization of the pseudo-peptide scaffold upon Cu(I) complexation. Considering that thioether functions are neutral sulfur donors, the stability constants measured by competition with ferrozine are quite large: log K approximate to 10.2-10.3. The CuT1,(2) complexes are significantly more stable that those formed with linear peptides, mimicking isolated Mets motifs MXMXXM of the Cu transport protein Ctr1 (log K approximate to 5-6). This may be attributed to the preorganized pseudo-peptide scaffold, which arranges the three neutral sulfur donors toward the metal center. Such moderate affinity Cu(I) chelators are interesting for applications in chelation therapy, for instance, to induce minimum disturbance of Cu homeostasis in Wilsons Disease treatments.
Kamal Nath - One of the best experts on this subject based on the ideXlab platform.
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a rare case of Wilsons Disease with zoophilia
American Journal of Psychiatry and Neuroscience, 2019Co-Authors: Prakash Barman, Madhurima Khasnobis, Kamal NathAbstract:Wilsons Disease also known as hepatolenticular degeneration is a autosomal recessive disorder, characterized by abnormal copper deposition in the liver, brain, and other tissues caused by mutation in the copper transporting gene ATP7B. Patients presents with neurological and hepatic disorder. Psychiatric manifestation are common along with movement disorder but its association with paraphilic disorders like zoophilia is very rare and there is practically no literature regarding this in North-Eatern India. In this article we report the unique case of a 21 year old boy from rural Assam suffering from Wilson’s Disease with multiple neuropsychiatric manifestations among which zoophilia was noteworthy. This case report highlights a rare and atypical association between an adolescent patient of Wilson Disease & zoophilia--- a relatively rare paraphilic disorder. A 21 year old boy presented in the Psychiatry emergency department in a tertiary care hospital with aggressive, disorganized behavior with reported sexual act with a cow. Examination of the patient also revealed massive organomegaly and K-F ring which on further investigation confirmed the diagnosis of Wilsons Disease. The occurrence of zoophilic behavior in Wilsons Disease is very rare and we have not come across any such report regarding this. To conclude, the association between copper deposition in specific brain areas due to Wilsons Disease and zoophilic behaviour we need further studies with better investigative modalities, which will in turn help in drawing an individualise treatment plan.