Prenyl sulfates as alkylating reagents for mercapto amino acids.

2008 ◽  
Vol 55 (4) ◽  
pp. 807-813 ◽  
Author(s):  
Sergey Maltsev ◽  
Olga Sizova ◽  
Natalia Utkina ◽  
Vladimir Shibaev ◽  
Tadeusz Chojnacki ◽  
...  
Keyword(s):  
Amino Acids ◽  
Alkylating Agents ◽  
Aqueous Systems ◽  
Thiol Compounds ◽  
Isoprene Unit ◽  
Alkylating Reagents

A new methodology for prenylation of thiol compounds has been developed. The approach is based on the use of prenyl sulfates as new reagents for S-prenylation of benzenethiol and cysteamine in aqueous systems. The C(10)-prenols geraniol and nerol that differ in the configuration (E or Z, correspondingly) of the alpha-isoprene unit were efficiently O-sulfated in the presence of a pyridine-SO(3') complex. The obtained geranyl and neryl sulfates were tested as alkylating agents. These compounds were chosen to reveal the influence of the alpha-isoprene unit configuration on their alkylation (prenylation) ability. S-Geranyl cysteine was prepared to demonstrate the applicability of this method for prenylation of peptides containing mercapto amino acids.

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

Efficient and chemoselective alkylation of amines/amino acids using alcohols as alkylating reagents under mild conditions

2010 ◽  
Vol 46 (41) ◽  
pp. 7834 ◽  
Author(s):  
Chu-Pei Xu ◽  
Zhen-Hua Xiao ◽  
Bi-Qin Zhuo ◽  
Yu-Huang Wang ◽  
Pei-Qiang Huang
Keyword(s):  
Amino Acids ◽  
Mild Conditions ◽  
Alkylating Reagents

ChemInform Abstract: Efficient and Chemoselective Alkylation of Amines/Amino Acids Using Alcohols as Alkylating Reagents under Mild Conditions.

ChemInform ◽  
2011 ◽  
Vol 42 (9) ◽  
pp. no-no
Author(s):  
Chu-Pei Xu ◽  
Zhen-Hua Xiao ◽  
Bi-Qin Zhuo ◽  
Yu-Huang Wang ◽  
Pei-Qiang Huang
Keyword(s):  
Amino Acids ◽  
Mild Conditions ◽  
Alkylating Reagents

scholarly journals The Aminopropylation of Bovine Serum Albumin

1967 ◽  
Vol 20 (1) ◽  
pp. 233 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Amino Acids ◽  
Alkylating Agents ◽  
Side Reactions ◽  
Contrast Reaction ◽  
Ph Values ◽  
Subsequent Hydrolysis ◽  
Positive Peak ◽  
State Of Affairs ◽  
Hydrolysis Of ◽  
Quantitative Recovery

After the reaction of reduced BSAt with BPA at pH 10�6 and subsequent hydrolysis of the protein with 6N HCl, only 40% of the lysine present in the unmodified protein can be accounted for on chromatographic analysis of the hydrolysate; a similar loss is observed of the SAPC into which the original cystine, which has totally disappeared, is presumably initially all converted. In place of these amino acids, a "neutral" ninhydrin-positive peak is observed which accounts approximately quantitatively for the missing lysine. The reaction at pH 8� 6 with IP A leads to a quantitative recovery of SAPC with no loss of lysine. In contrast, reaction for the same times at both pH values with BEA leads to quantitative recovery of all amino acids including SAEC. Although the reaction ofIP A with thiols at pH 8�6 is very slow compared with that of other alkylating agents, the relative absence of side reactions may be compared with the state of affairs when methyl iodide is used for an equivalent period in the same relative quantities, when there is extensive alteration of lysine, histidine, methionine, and S-methylcysteine.

scholarly journals Distributed Drug Discovery, Part 2: Global Rehearsal of Alkylating Agents for the Synthesis of Resin-Bound Unnatural Amino Acids and Virtual D3Catalog Construction

2009 ◽  
Vol 11 (1) ◽  
pp. 14-33 ◽  
Author(s):  
William L. Scott ◽  
Jordi Alsina ◽  
Christopher O. Audu ◽  
Evgenii Babaev ◽  
Linda Cook ◽  
...  
Keyword(s):  
Amino Acids ◽  
Drug Discovery ◽  
Unnatural Amino Acids ◽  
Alkylating Agents
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