The Experts below are selected from a list of 165 Experts worldwide ranked by ideXlab platform
Chérine Bechara - One of the best experts on this subject based on the ideXlab platform.
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tryptophan within Basic Peptide sequences triggers glycosaminoglycan dependent endocytosis
The FASEB Journal, 2013Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne BurlinaAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased...
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Tryptophan within Basic Peptide sequences triggers glycosaminoglycan-dependent endocytosis
The FASEB Journal, 2012Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne Burlina, Isabel D Alves, Olivier Lequin, Sandrine SaganAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased 2 times with 1 Trp residue, 10 times with 2 Trp residues, and 20 times with 3 Trp residues, compared with +6 Peptides with no Trp residues. Therefore, Trp residues represent molecular determinants in Basic Peptide sequences not only for direct membrane translocation but also for efficient endocytosis through GAGs.
Fabienne Burlina - One of the best experts on this subject based on the ideXlab platform.
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tryptophan within Basic Peptide sequences triggers glycosaminoglycan dependent endocytosis
The FASEB Journal, 2013Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne BurlinaAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased...
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Tryptophan within Basic Peptide sequences triggers glycosaminoglycan-dependent endocytosis
The FASEB Journal, 2012Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne Burlina, Isabel D Alves, Olivier Lequin, Sandrine SaganAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased 2 times with 1 Trp residue, 10 times with 2 Trp residues, and 20 times with 3 Trp residues, compared with +6 Peptides with no Trp residues. Therefore, Trp residues represent molecular determinants in Basic Peptide sequences not only for direct membrane translocation but also for efficient endocytosis through GAGs.
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A Basic Peptide derived from the HARP C-terminus inhibits anchorage-independent growth of DU145 prostate cancer cells.
Experimental Cell Research, 2007Co-Authors: Oya Bermek, Fabienne Burlina, Zoi Diamantopoulou, Apostolos Polykratis, Célia Dos Santos, Yamina Hamma-kourbali, Jean Delbé, Gérard Chassaing, David G. Fernig, Pagnagiotis KatsorisAbstract:Heparin affin regulatory Peptide (HARP) is an 18 kDa heparin-binding protein that plays a key role in tumor growth. We showed previously that the synthetic Peptide P(111-136) composed of the last 26 HARP amino acids inhibited HARP-induced mitogenesis. Here, to identify the exact molecular domain involved in HARP inhibition, we investigated the effect of the shorter Basic Peptide P(122-131) on DU145 cells, which express HARP and its receptor protein tyrosine phosphatase beta/zeta (RPTPbeta/zeta). P(122-131) was not cytotoxic; it dose-dependently inhibited anchorage-independent growth of DU145 cells. Binding studies using biotinylated P(122-131) indicated that this Peptide interfered with HARP binding to DU145 cells. Investigation of the mechanisms involved suggested interference, under anchorage-independent conditions, of P(122-131) with a HARP autocrine loop in an RPTPbeta/zeta-dependent fashion. Thus, P(122-131) may hold potential for the treatment of disorders involving RPTPbeta/zeta.
Yefim Zaltsman - One of the best experts on this subject based on the ideXlab platform.
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tryptophan within Basic Peptide sequences triggers glycosaminoglycan dependent endocytosis
The FASEB Journal, 2013Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne BurlinaAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased...
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Tryptophan within Basic Peptide sequences triggers glycosaminoglycan-dependent endocytosis
The FASEB Journal, 2012Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne Burlina, Isabel D Alves, Olivier Lequin, Sandrine SaganAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased 2 times with 1 Trp residue, 10 times with 2 Trp residues, and 20 times with 3 Trp residues, compared with +6 Peptides with no Trp residues. Therefore, Trp residues represent molecular determinants in Basic Peptide sequences not only for direct membrane translocation but also for efficient endocytosis through GAGs.
Manjula Pallerla - One of the best experts on this subject based on the ideXlab platform.
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tryptophan within Basic Peptide sequences triggers glycosaminoglycan dependent endocytosis
The FASEB Journal, 2013Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne BurlinaAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased...
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Tryptophan within Basic Peptide sequences triggers glycosaminoglycan-dependent endocytosis
The FASEB Journal, 2012Co-Authors: Chérine Bechara, Manjula Pallerla, Yefim Zaltsman, Fabienne Burlina, Isabel D Alves, Olivier Lequin, Sandrine SaganAbstract:Deciphering the structural requirements and mechanisms for internalization of cell-penetrating Peptides (CPPs) is required to improve their delivery efficiency. Herein, a unique role of tryptophan (Trp) residues in the interaction and structuring of cationic CPP sequences with glycosaminoglycans (GAGs) has been characterized, in relation with cell internalization. Using isothermal titration calorimetry, circular dichroism, NMR, mass spectrometry, and phase-contrast microscopy, we compared the interaction of 7 Basic CPPs with 5 classes of GAGs. We found that the affinity of CPPs for GAGs increases linearly with the number of Trp residues, from 30 nM for a penetratin analog with 1 Trp residue to 1.5 nM for a penetratin analog with 6 Trp residues for heparin (HI); Peptides with Trp residues adopt a predominantly β-strand structure in complex with HI and form large, stable β-sheet aggregates with GAGs; and in the absence of any cytotoxicity effect, the quantity of Peptide internalized into CHO cells increased 2 times with 1 Trp residue, 10 times with 2 Trp residues, and 20 times with 3 Trp residues, compared with +6 Peptides with no Trp residues. Therefore, Trp residues represent molecular determinants in Basic Peptide sequences not only for direct membrane translocation but also for efficient endocytosis through GAGs.
Isaac N Pessah - One of the best experts on this subject based on the ideXlab platform.
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chemical synthesis and characterization of maurocalcine a scorpion toxin that activates ca2 release channel ryanodine receptors
FEBS Letters, 2000Co-Authors: Ziad Fajloun, Riadh Kharrat, Lili Chen, C Lecomte, E Di Luccio, Delphine Bichet, El M Ayeb, H Rochat, Paul D Allen, Isaac N PessahAbstract:Abstract Maurocalcine is a novel toxin isolated from the venom of the chactid scorpion Scorpio maurus palmatus. It is a 33-mer Basic Peptide cross-linked by three disulfide bridges, which shares 82% sequence identity with imperatoxin A, a scorpion toxin from the venom of Pandinus imperator. Maurocalcine is peculiar in terms of structural properties since it does not possess any consensus motif reported so far in other scorpion toxins. Due to its low concentration in venom (0.5% of the proteins), maurocalcine was chemically synthesized by means of an optimized solid-phase method, and purified after folding/oxidation by using both C18 reversed-phase and ion exchange high-pressure liquid chromatographies. The synthetic product (sMCa) was characterized. The half-cystine pairing pattern of sMCa was identified by enzyme-based cleavage and Edman sequencing. The pairings were Cys3-Cys17, Cys10-Cys21, and Cys16-Cys32. In vivo, the sMCa was lethal to mice following intracerebroventricular inoculation (LD50, 20 μg/mouse). In vitro, electrophysiological experiments based on recordings of single channels incorporated into planar lipid bilayers showed that sMCa potently and reversibly modifies channel gating behavior of the type 1 ryanodine receptor by inducing prominent subconductance behavior.