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M3i
Modèles Insectes d’Immunité Innée
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2000
Casimir J R, Iterbeke K, Nest W Van Den, Trescol-Biémont M C, Dumortier H, Muller S, Gerlier D, Rabourdin-Combe C, Tourwé D, Paris J
Conformational restriction of the Tyr53 side-chain in the decapeptide HE Article de journal
Dans: The Journal of Peptide Research: Official Journal of the American Peptide Society, vol. 56, no. 6, p. 398–408, 2000, ISSN: 1397-002X.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid Sequence, Animals, Antigen, Antigen-Presenting Cells, B-Lymphocytes, Chemical, Chickens, Dumortier, I2CT, Major Histocompatibility Complex, Mice, Models, Molecular Sequence Data, Muramidase, Peptide Biosynthesis, Peptides, Phenylalanine, Protein Binding, Protein Conformation, Receptors, T-Cell, Team-Dumortier, Temperature, Tyrosine
@article{casimir_conformational_2000,
title = {Conformational restriction of the Tyr53 side-chain in the decapeptide HE},
author = {J R Casimir and K Iterbeke and W Van Den Nest and M C Trescol-Biémont and H Dumortier and S Muller and D Gerlier and C Rabourdin-Combe and D Tourwé and J Paris},
doi = {10.1034/j.1399-3011.2000.00777.x},
issn = {1397-002X},
year = {2000},
date = {2000-12-01},
journal = {The Journal of Peptide Research: Official Journal of the American Peptide Society},
volume = {56},
number = {6},
pages = {398--408},
abstract = {A series of conformationally restricted analogs of the hen egg lysozyme (HEL) decapeptide 52-61 in which the conformationally flexible Tyr53 residue was replaced by several more constrained tyrosine and phenylalanine analogs was prepared. Among these tyrosine and phenylalanine analogs were 1,2,3,4-tetrahydro-7-hydroxyisoquinoline-3-carboxylic acid (Htc), 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), 4-amino- 1,2,4,5-tetrahydro-8-hydroxy-2-benzazepine-3-one (Hba), 4-amino-1,2,4,5-tetrahydro-2-benzazepine-3-one (Aba), 2-amino-6-hydroxytetralin-2-carboxylic acid (Hat) and 2-amino-5-hydroxyindan-2-carboxylic acid (Hai) in which the rotations around Calpha-Cbeta and Cbeta-Cgamma were restricted because of cyclization of the side-chain to the backbone. Synthesis of Pht-Hba-Gly-OH using a modification of the Flynn and de Laszlo procedure is described. Analogs of beta-methyltyrosine (beta-MeTyr) in which the side-chains were biased to particular side-chain torsional angles because of substitution at the beta-hydrogens were also prepared. These analogs of HEL[52-61] peptide were tested for their ability to bind to the major histocompatibility complex class II I-Ak molecule and to be recognized in this context by two T-cell hybridomas, specific for the parent peptide HEL[52-61]. The data showed that the conformation and also the configuration of the Tyr53 residue influenced both the binding of the peptide to I-Ak and the recognition of the peptide/I-Ak complex by a T-cell receptor.},
keywords = {Amino Acid Sequence, Animals, Antigen, Antigen-Presenting Cells, B-Lymphocytes, Chemical, Chickens, Dumortier, I2CT, Major Histocompatibility Complex, Mice, Models, Molecular Sequence Data, Muramidase, Peptide Biosynthesis, Peptides, Phenylalanine, Protein Binding, Protein Conformation, Receptors, T-Cell, Team-Dumortier, Temperature, Tyrosine},
pubstate = {published},
tppubtype = {article}
}
A series of conformationally restricted analogs of the hen egg lysozyme (HEL) decapeptide 52-61 in which the conformationally flexible Tyr53 residue was replaced by several more constrained tyrosine and phenylalanine analogs was prepared. Among these tyrosine and phenylalanine analogs were 1,2,3,4-tetrahydro-7-hydroxyisoquinoline-3-carboxylic acid (Htc), 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid (Tic), 4-amino- 1,2,4,5-tetrahydro-8-hydroxy-2-benzazepine-3-one (Hba), 4-amino-1,2,4,5-tetrahydro-2-benzazepine-3-one (Aba), 2-amino-6-hydroxytetralin-2-carboxylic acid (Hat) and 2-amino-5-hydroxyindan-2-carboxylic acid (Hai) in which the rotations around Calpha-Cbeta and Cbeta-Cgamma were restricted because of cyclization of the side-chain to the backbone. Synthesis of Pht-Hba-Gly-OH using a modification of the Flynn and de Laszlo procedure is described. Analogs of beta-methyltyrosine (beta-MeTyr) in which the side-chains were biased to particular side-chain torsional angles because of substitution at the beta-hydrogens were also prepared. These analogs of HEL[52-61] peptide were tested for their ability to bind to the major histocompatibility complex class II I-Ak molecule and to be recognized in this context by two T-cell hybridomas, specific for the parent peptide HEL[52-61]. The data showed that the conformation and also the configuration of the Tyr53 residue influenced both the binding of the peptide to I-Ak and the recognition of the peptide/I-Ak complex by a T-cell receptor.
1977
Hoffmann Danièle, Brehelin M, Hoffmann Jules A
First results of the antibacterial defense reactions of Locusta migratoria larva and imago Article de journal
Dans: Ann Parasitol Hum Comp, vol. 52, no. 1, p. 87–88, 1977, ISSN: 0003-4150.
BibTeX | Étiquettes: Animals, Bacillus thuringiensis, bacteria, Cellular, Grasshoppers, Hematopoietic System, Hemocytes, Hemolymph, hoffmann, Immunity, Larva, M3i, Muramidase
@article{hoffmann_first_1977,
title = {First results of the antibacterial defense reactions of Locusta migratoria larva and imago},
author = {Danièle Hoffmann and M Brehelin and Jules A Hoffmann},
issn = {0003-4150},
year = {1977},
date = {1977-02-01},
journal = {Ann Parasitol Hum Comp},
volume = {52},
number = {1},
pages = {87--88},
keywords = {Animals, Bacillus thuringiensis, bacteria, Cellular, Grasshoppers, Hematopoietic System, Hemocytes, Hemolymph, hoffmann, Immunity, Larva, M3i, Muramidase},
pubstate = {published},
tppubtype = {article}
}