ChemInform Abstract: INTRODUCTION OF 9-FLUORENYLMETHYLOXYCARBONYL, TRICHLOROETHOXYCARBONYL, AND BENZYLOXYCARBONYL AMINE PROTECTING GROUPS INTO O-UNPROTECTED HYDROXY AMINO ACIDS USING SUCCINIMIDYL CARBONATES

1982 ◽  
Vol 13 (36) ◽  
Author(s):  
A. PAQUET
Keyword(s):  
Amino Acids ◽  
Protecting Groups ◽  
Hydroxy Amino

Vasopressin and oxytocin analogs with interchanged sequence of amino acids in positions 7 and 8. synthesis and biological effects

1981 ◽  
Vol 46 (9) ◽  
pp. 2136-2139 ◽  
Author(s):  
Ivo Bláha ◽  
Viktor Krchňák ◽  
Milan Zaoral
Keyword(s):  
Amino Acids ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
Biological Effects ◽  
Free Flow ◽  
Protecting Groups ◽  
Pressor Effect ◽  
Phase Synthesis ◽  
Antidiuretic Effect

p-Toluenesulfonyl-S-benzylcysteinyl-tyrosyl-phenylalanyl-glutaminyl-asparaginyl-S-benzylcysteinyl-NG-p-toluenesulfanylarginyl-prolyl-glycineamide (I) and S-benzylcysteinyl-tyrosyl-isoleucyl-glutaminyl-asparaginyl-S-benzylcysteinyl-leucyl-prolyl-glycine amide (III) were prepared by solid phase synthesis. After removal of the protecting groups, closure of the disulfide ring, and purification by continuous free-flow electrophoresis [arginine7, proline8]vasopressin (II) and [leucine7, proline8]oxytocin (IV) were obtained. The antidiuretic effect of II is markedly higher than its pressor effect; IV possesses c. 6% of the uterotonic and c. 10% of the galactogogous effect of oxytocin.

scholarly journals Amino Acids and Peptides. LIV. Application of 2-Adamantyl Derivatives as Protecting Groups to the Synthesis of Peptide Fragments Related to Sulfolobus solifataricus Ribnuclease. I.

1999 ◽  
Vol 47 (8) ◽  
pp. 1089-1096 ◽  
Author(s):  
Yoshio OKADA ◽  
Shima JOSHI ◽  
Noriyuki SHINTOMI ◽  
Yukihiro KONDO ◽  
Yuko TSUDA ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protecting Groups ◽  
Peptide Fragments

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.

Monosaccharides as O-glycosyl leaving groups from 3-hydroxy amino acids during base-catalyzed elimination

1970 ◽  
Vol 13 (1) ◽  
pp. 63-74 ◽  
Author(s):  
J.R. Vercellotti ◽  
Nancy Nienaber ◽  
Chang Ching Jen
Keyword(s):  
Amino Acids ◽  
Hydroxy Amino ◽  
Leaving Groups
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