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10.1002/bip.22505 http://scihub22266oqcxt.onion/10.1002/bip.22505 C4107132!4107132 !24839139     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24839139 &cmd=llinks): Failed to open stream: HTTP request failed! 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Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide |pdf=|usr=}}{{24839139 }} gab.com Text Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide JO: Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=24839139 #FOAvip Protein-protein interactions are part of a large number of signaling networks and potential targets for drug development. However, discovering molecules that can specifically inhibit such interactions is a major challenge. S100B, a calcium-regulated protein, plays a crucial role in the proliferation of melanoma cells through protein-protein interactions. In this article, we report the design and development of a bidentate conformationally constrained peptide against dimeric S100B based on a natural tight-binding peptide, TRTK-12. The helical conformation of the peptide was constrained by the substitution of ?-amino isobutyric acid--an amino acid having high helical propensity--in positions which do not interact with S100B. A branched bidentate version of the peptide was bound to S100B tightly with a dissociation constant of 8 nM. When conjugated to a cell-penetrating peptide, it caused growth inhibition and rapid apoptosis in melanoma cells. The molecule exerts antiproliferative action through simultaneous inhibition of key growth pathways, including reactivation of wild-type p53 and inhibition of Akt and STAT3 phosphorylation. The apoptosis induced by the bidentate constrained helix is caused by direct migration of p53 to mitochondria. At moderate intravenous dose, the peptide completely inhibits melanoma growth in a mouse model without any significant observable toxicity. The specificity was shown by lack of ability of a double mutant peptide to cause tumor regression at the same dose level. The methodology described here for direct protein-protein interaction inhibition may be effective for rapid development of inhibitors against relatively weak protein-protein interactions for de novo drug development. Twit Text FOAVip Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide ????Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=24839139 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24839139 #FOAvip English Wikipedia <ref>{{Cite pmid|24839139 }}</ref> Simultaneous inhibition of key growth pathways in melanoma cells and tumor regression by a designed bidentate constrained helical peptide #MMPMID24839139 Dhar A ; Mallick S ; Ghosh P ; Maiti A ; Ahmed I ; Bhattacharya S ; Mandal T ; Manna A ; Roy K ; Singh S ; Nayak DK ; Wilder PT ; Markowitz J ; Weber D ; Ghosh MK ; Chattopadhyay S ; Guha R ; Konar A ; Bandyopadhyay S ; Roy S Biopolymers 2014[Jul]; 102 (4 ): 344-58 PMID24839139 show ga Protein-protein interactions are part of a large number of signaling networks and potential targets for drug development. However, discovering molecules that can specifically inhibit such interactions is a major challenge. S100B, a calcium-regulated protein, plays a crucial role in the proliferation of melanoma cells through protein-protein interactions. In this article, we report the design and development of a bidentate conformationally constrained peptide against dimeric S100B based on a natural tight-binding peptide, TRTK-12. The helical conformation of the peptide was constrained by the substitution of ?-amino isobutyric acid--an amino acid having high helical propensity--in positions which do not interact with S100B. A branched bidentate version of the peptide was bound to S100B tightly with a dissociation constant of 8 nM. When conjugated to a cell-penetrating peptide, it caused growth inhibition and rapid apoptosis in melanoma cells. The molecule exerts antiproliferative action through simultaneous inhibition of key growth pathways, including reactivation of wild-type p53 and inhibition of Akt and STAT3 phosphorylation. The apoptosis induced by the bidentate constrained helix is caused by direct migration of p53 to mitochondria. At moderate intravenous dose, the peptide completely inhibits melanoma growth in a mouse model without any significant observable toxicity. The specificity was shown by lack of ability of a double mutant peptide to cause tumor regression at the same dose level. The methodology described here for direct protein-protein interaction inhibition may be effective for rapid development of inhibitors against relatively weak protein-protein interactions for de novo drug development. |Amino Acid Sequence [MESH] |Animals [MESH] |Blotting, Western [MESH] |CapZ Actin Capping Protein/*chemistry/*pharmacology [MESH] |Cell Line, Tumor [MESH] |Cell Proliferation/drug effects [MESH] |Cell Survival [MESH] |Disease Models, Animal [MESH] |Humans [MESH] |Melanoma/*pathology [MESH] |Mice [MESH] |Microscopy, Phase-Contrast [MESH] |Molecular Sequence Data [MESH] |Peptide Fragments/*chemistry/*pharmacology [MESH] |Protein Binding [MESH] |Protein Structure, Secondary [MESH] |Remission Induction [MESH] |Signal Transduction/drug effects [MESH] |Temperature [MESH]Simultaneous inhibition of key growth pathways in melanoma cells and t(epmc).pdf DeepDyve Pubget Overpricing