Amino acid chalcogen analogues as tools in peptide and protein research. (19th December 2019)

• Record Type: Journal Article
• Authors: Moroder, Luis; Musiol, Hans‐Jürgen
• Is Part Of: Journal of peptide science. Volume 26:Number 2(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-12-19
• Subjects: methoxinine -- peptides -- proteins -- redox potentials -- selenocysteine and tellurocysteine -- selenomethionine and telluromethionine -- β‐selenienylalanine and β‐tellurienylalanine -- β‐thienylalanine -- β‐(thienopyrrolyl)‐ and β‐(selenolopyrrolyl)‐alanine; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.3232
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium element. In the methionine series, only the sulfur‐containing methionine is a proteinogenic amino acid, while selenomethionine and telluromethionine are natural amino acids that are incorporated into proteins most probably because of the tolerance of the methionyl‐ t RNA synthetase; so far, methoxinine the oxygen analogue has not been discovered in natural compounds. Similarly, the chalcogen analogues of tryptophan and phenylalanine in which the benzene ring has been replaced by the largely isosteric thiophene, selenophene, and more recently, even tellurophene are fully synthetic mimics that are incorporated with more or less efficiency into proteins via the related tryptophanyl‐ and phenylalanyl‐ t RNA synthetases, respectively. In the serine/cysteine series, also selenocysteine is a proteinogenic amino acid that is inserted into proteins by a special translation mechanism, while the tellurocysteine is again most probably incorporated into proteins by the tolerance of the cysteinyl‐ t RNA synthetase. For research purposes, all of these natural and synthetic chalcogen amino acids have been extensively applied in peptide and protein research to exploit their different physicochemical properties for modulating structural and functional properties in synthetic peptides and r DNA expressed proteins as discussed in the following review. Abstract : Although the chemistry of the chalcogen members oxygen, sulfur, selenium, and the metalloid tellurium are closely intertwined, the respective physicochemical aspects differ significantly imparting specific properties to the chalcogen‐containing side chains of proteinogenic and synthetic amino acids. These differences define specific roles in vivo and open interesting and promising applications of related peptides and proteins as analytical probes, advanced reagents, and even novel therapeutics.