Selective Fluorination of Hydroxy Amines and Hydroxy Amino Acids with Sulfur Tetrafluoride in Liquid Hydrogen Fluoride

1975 ◽  
Vol 40 (25) ◽  
pp. 3808-3809 ◽  
Author(s):  
J Kollonitsch ◽  
S Marburg ◽  
Leroy Perkins
Keyword(s):  
Amino Acids ◽  
Hydrogen Fluoride ◽  
Liquid Hydrogen ◽  
Hydroxy Amino ◽  
Sulfur Tetrafluoride

Synthesis of oxytocin, arginine-vasopressin and its deamino-analogue using 2,4,6-trimethylbenzyl group for protection of the cysteine sulfur

1981 ◽  
Vol 46 (1) ◽  
pp. 286-299 ◽  
Author(s):  
František Brtník ◽  
Milan Krojidlo ◽  
Tomislav Barth ◽  
Karel Jošt
Keyword(s):  
Peptide Synthesis ◽  
Hydrogen Fluoride ◽  
Sulfur Atom ◽  
Arginine Vasopressin ◽  
Liquid Hydrogen ◽  
Trifluoromethanesulfonic Acid ◽  
Protecting Groups ◽  
Mild Conditions

Preparation of oxytocin, arginine-vasopressin and its deamino-analogue serves as an example of use of 2,4,6-trimethylbenzyl group for protection of the cysteine sulfur atom in the peptide synthesis. This modified benzyl group is sufficiently stable under conditions of solvolytic removal of common amino-protecting groups and it can be cleaved off under mild conditions with liquid hydrogen fluoride or trifluoromethanesulfonic acid.

scholarly journals Studies on Hydroxy Amino Acids. II. The Optical Resolution of α-Amino-β-hydroxy-γ-benzyloxybutyric Acid

1969 ◽  
Vol 42 (9) ◽  
pp. 2720-2722 ◽  
Author(s):  
Kenji Okawa ◽  
Kiyotaka Hori ◽  
Katsutoshi Hirose ◽  
Yasuo Nakagawa
Keyword(s):  
Amino Acids ◽  
Optical Resolution ◽  
Hydroxy Amino

Specific sulfonation of tyrosine, tryptophan and hydroxy-amino acids in peptides

1979 ◽  
Vol 581 (2) ◽  
pp. 276-282 ◽  
Author(s):  
A. Previero ◽  
J-C. Cavadore ◽  
J. Torreilles ◽  
M-A. Coletti-Previero
Keyword(s):  
Amino Acids ◽  
Hydroxy Amino

scholarly journals The sustainability of interactions between the orexin-1 receptor and β-arrestin-2 is defined by a single C-terminal cluster of hydroxy amino acids and modulates the kinetics of ERK MAPK regulation

2005 ◽  
Vol 387 (3) ◽  
pp. 573-584 ◽  
Author(s):  
Sandra MILASTA ◽  
Nicholas A. EVANS ◽  
Laura ORMISTON ◽  
Shelagh WILSON ◽  
Robert J. LEFKOWITZ ◽  
...  
Keyword(s):  
Amino Acids ◽  
Fluorescent Protein ◽  
Weak Interactions ◽  
Dependent Manner ◽  
Wild Type ◽  
Erk Mapk ◽  
Hydroxy Amino ◽  
C Terminus ◽  
Green Fluorescent ◽  
Kinetics Of

The orexin-1 receptor interacts with β-arrestin-2 in an agonist-dependent manner. In HEK-293T cells, these two proteins became co-internalized into acidic endosomes. Truncations from the C-terminal tail did not prevent agonist-induced internalization of the orexin-1 receptor or alter the pathway of internalization, although such mutants failed to interact with β-arrestin-2 in a sustained manner or produce its co-internalization. Mutation of a cluster of three threonine and one serine residue at the extreme C-terminus of the receptor greatly reduced interaction and abolished co-internalization of β-arrestin-2–GFP (green fluorescent protein). Despite the weak interactions of this C-terminally mutated form of the receptor with β-arrestin-2, studies in wild-type and β-arrestin-deficient mouse embryo fibroblasts confirmed that agonist-induced internalization of this mutant required expression of a β-arrestin. Although without effect on agonist-mediated elevation of intracellular Ca2+ levels, the C-terminally mutated form of the orexin-1 receptor was unable to sustain phosphorylation of the MAPKs (mitogen-activated protein kinases) ERK1 and ERK2 (extracellular-signal-regulated kinases 1 and 2) to the same extent as the wild-type receptor. These studies indicate that a single cluster of hydroxy amino acids within the C-terminal seven amino acids of the orexin-1 receptor determine the sustainability of interaction with β-arrestin-2, and indicate an important role of β-arrestin scaffolding in defining the kinetics of orexin-1 receptor-mediated ERK MAPK activation.

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