蛋白质生成氨基酸的特征、作用及手性分析

IF 0.7 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
N. Ayon
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引用次数: 15

摘要

氨基酸(AAs)是重要的生物分子,在原核和真核生物系统中都具有多种功能。有22种天然氨基酸,其中20种常见的氨基酸出现在遗传密码中,被称为蛋白质生成氨基酸,它们是蛋白质的组成部分。蛋白质原氨基酸以两种异构体形式存在(甘氨酸除外),其生物活性通常归因于特定的立体异构体。蛋白质中发现的大多数氨基酸主要是l - aa。少量的d -氨基酸存在于细菌细胞壁、一些海洋无脊椎动物和高等生物中,包括青蛙、蜗牛、蜘蛛、老鼠、鸡和人。除了它们在蛋白质合成中的作用外,不同的蛋白质生成氨基酸立体异构体已经被发现发挥重要的生物学作用,要么作为无数其他生物活性分子的前体,要么通过指示几种生物现象,即作为不同生理条件的标记。鉴于L-和d -氨基酸(AAs)的生物学重要性,改进的分析方法对它们的分辨率和准确定量仍然是人们关注的焦点。复杂生物基质中氨基酸的手性分析提出了许多分析挑战,这些挑战由于蛋白质原氨基酸立体异构体的极性和电离效率的巨大差异而加剧。迄今为止,报道了各种分析方法用于手性氨基酸分析,包括色谱,光谱,酶,流体,电泳和微生物技术。固定相、衍生化化学和仪器的进步有助于实现基线分离和准确检测不同基质中痕量的蛋白质原氨基酸立体异构体。然而,液相和气相色谱联用质谱分析方法在可行性和性能方面仍然是手性氨基酸分析中最流行的平台。本文综述了蛋白质氨基酸立体异构体的不同物理化学和生物学特征和功能,并列举了迄今为止报道的各种基于色谱和质谱的分析方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Features, roles and chiral analyses of proteinogenic amino acids
Amino acids (AAs) are important biomolecules responsible for plethora of functions in both prokaryotic and eukaryotic systems. There are 22 naturally occurring amino acids, among which 20 common amino acids appear in the genetic code and known as proteinogenic amino acids, which are the building blocks of proteins. Proteinogenic amino acids exist in two isomeric forms (except glycine) and the biological activity is often attributed to a specific stereoisomer. Most of the amino acids found in protein is predominantly L-AAs. A few D-amino acids can be found in bacterial cell wall, some marine invertebrates and higher organisms including frog, snail, spider, rat, chicken and human. Besides their role in protein synthesis, different proteinogenic amino acid stereoisomers have found to perform important biological roles either by functioning as precursors of a myriad of other bioactive molecules or by indicating several biological phenomena i.e. acting as markers for different physiological conditions. Given the biological importance of L- and D-amino acids (AAs), improved analytical methods for their resolution and accurate quantification remain of keen interest. Chiral analysis of amino acids in complex biological matrices poses numerous analytical challenges that are exacerbated by broad differences in polarity and ionization efficiencies of the proteinogenic amino acid stereoisomers. To date, various analytical methods are reported for chiral amino acid analysis including chromatographic, spectrometric, enzymatic, fluidic, electrophoretic and microbiological techniques. Advances in stationary phase, derivatization chemistry and instrumentation contributed to achieving baseline separation and accurate detection of trace levels of proteinogenic amino acids stereoisomers in different matrices. However, liquid and gas chromatography coupled to mass spectrometry based analytical methods remain the most popular platform in chiral amino acid analysis in terms of feasibility and performance. This review discusses different physicochemical and biological features and functions of proteinogenic amino acid stereoisomers and lists a variety of established chromatography and mass spectrometry based analytical methods for their analysis reported to date.
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来源期刊
AIMS Molecular Science
AIMS Molecular Science BIOCHEMISTRY & MOLECULAR BIOLOGY-
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