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Title: A Better Understanding of Protein Structure and Function by the Synthesis and Incorporation of Selenium- and Tellurium Containing Tryptophan Analogs

Abstract

Unnatural heavy metal-containing amino acid analogs have shown to be very important in the analysis of protein structure, using methods such as X-ray crystallography, mass spectroscopy, and NMR spectroscopy. Synthesis and incorporation of selenium-containing methionine analogs has already been shown in the literature however with some drawbacks due to toxicity to host organisms. Thus synthesis of heavy metal tryptophan analogs should prove to be more effective since the amino acid tryptophan is naturally less abundant in many proteins. For example, bioincorporation of β-seleno[3,2-b]pyrrolyl-L-alanine ([4,5]SeTrp) and β-selenolo[2,3-b]pyrrolyl-L-alanine ([6,7]SeTrp) has been shown in the following proteins without structural or catalytic perturbations: human annexin V, barstar, and dihydrofolate reductase. The reported synthesis of these Se-containing analogs is currently not efficient for commercial purposes. Thus a more efficient, concise, high-yield synthesis of selenotryptophan, as well as the corresponding, tellurotryptophan, will be necessary for wide spread use of these unnatural amino acid analogs. This research will highlight our progress towards a synthetic route of both [6,7]SeTrp and [6,7]TeTrp, which ultimately will be used to study the effect on the catalytic activity of Lignin Peroxidase (LiP).

Authors:
 [1];  [1];  [1];  [2];  [2]
  1. Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Bioscience Division; Belmont Univ., Nashville, TN (United States). Dept. of Chemistry and Physics
  2. Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Bioscience Division
Publication Date:
Research Org.:
Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
Contributing Org.:
Belmont Univ., Nashville, TN (United States)
OSTI Identifier:
1304806
Report Number(s):
LA-UR-16-26338
DOE Contract Number:
AC52-06NA25396
Resource Type:
Technical Report
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Biological Science

Citation Formats

Helmey, Sherif Samir, Rice, Ambrose Eugene, Hatch, Duane Michael, Silks, Louis A., and Marti-Arbona, Ricardo. A Better Understanding of Protein Structure and Function by the Synthesis and Incorporation of Selenium- and Tellurium Containing Tryptophan Analogs. United States: N. p., 2016. Web. doi:10.2172/1304806.
Helmey, Sherif Samir, Rice, Ambrose Eugene, Hatch, Duane Michael, Silks, Louis A., & Marti-Arbona, Ricardo. A Better Understanding of Protein Structure and Function by the Synthesis and Incorporation of Selenium- and Tellurium Containing Tryptophan Analogs. United States. doi:10.2172/1304806.
Helmey, Sherif Samir, Rice, Ambrose Eugene, Hatch, Duane Michael, Silks, Louis A., and Marti-Arbona, Ricardo. Wed . "A Better Understanding of Protein Structure and Function by the Synthesis and Incorporation of Selenium- and Tellurium Containing Tryptophan Analogs". United States. doi:10.2172/1304806. https://www.osti.gov/servlets/purl/1304806.
@article{osti_1304806,
title = {A Better Understanding of Protein Structure and Function by the Synthesis and Incorporation of Selenium- and Tellurium Containing Tryptophan Analogs},
author = {Helmey, Sherif Samir and Rice, Ambrose Eugene and Hatch, Duane Michael and Silks, Louis A. and Marti-Arbona, Ricardo},
abstractNote = {Unnatural heavy metal-containing amino acid analogs have shown to be very important in the analysis of protein structure, using methods such as X-ray crystallography, mass spectroscopy, and NMR spectroscopy. Synthesis and incorporation of selenium-containing methionine analogs has already been shown in the literature however with some drawbacks due to toxicity to host organisms. Thus synthesis of heavy metal tryptophan analogs should prove to be more effective since the amino acid tryptophan is naturally less abundant in many proteins. For example, bioincorporation of β-seleno[3,2-b]pyrrolyl-L-alanine ([4,5]SeTrp) and β-selenolo[2,3-b]pyrrolyl-L-alanine ([6,7]SeTrp) has been shown in the following proteins without structural or catalytic perturbations: human annexin V, barstar, and dihydrofolate reductase. The reported synthesis of these Se-containing analogs is currently not efficient for commercial purposes. Thus a more efficient, concise, high-yield synthesis of selenotryptophan, as well as the corresponding, tellurotryptophan, will be necessary for wide spread use of these unnatural amino acid analogs. This research will highlight our progress towards a synthetic route of both [6,7]SeTrp and [6,7]TeTrp, which ultimately will be used to study the effect on the catalytic activity of Lignin Peroxidase (LiP).},
doi = {10.2172/1304806},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Wed Aug 17 00:00:00 EDT 2016},
month = {Wed Aug 17 00:00:00 EDT 2016}
}

Technical Report:

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