Dishen Kumar Banjara, Srishti Dutta, Abhilash Pandey, Devanand Sahu, Vanshika Sharma and Goutam Kumar Patra* Pages 1 - 21 ( 21 )
Due to the biological importance of amino acids, the development of optical probes for these compounds has become a popular research topic in recent years. The amino acid fluorescence or colorimetric sensors are organized according to the reactions the amino acids go through and the related structural classification. Works on reaction-based chemosensors are categorized as either imine formation, Michael addition, thiazinane or thiazolidine formation, cleavage of a sulfonate ester, cleavage of a disulfide, metal complexes-displace coordination, or other mechanisms depending on the mechanisms between sensors and amino acids.
Amino acids (AA), which comprise most proteins, are small molecules with a wide range of functional side-chain groups. Amino acids, therefore, have a variety of roles in physiological processes. Histidine (His), a member of this family, is required for tissue growth and repair as well as for weight gain. Lysine (Lys), another member of this family, is intimately linked to the Krebs-Henseleit cycle and polyamine synthesis, and an adequate amount of lysine in the diet is necessary for animals' metabolic processes and weight gain. Because it controls the transfer of metal elements in biological bases, tryptophan (Trp) is crucial to biological processes like protein synthesis, animal growth, and plant development.
The majority of proteins are composed of amino acids (AA), which are tiny molecules with a variety of functional side chain groups. As a result, amino acids play a number of different roles in physiological processes. This family member's histidine (His) is necessary for weight gain, tissue growth, and repair. Another member of this family, lysine (Lys), is crucial for the Krebs-Henseleit cycle and polyamine production, and animals' metabolic activities and weight gain depend on appropriate lysine intake. Tryptophan (Trp) is an essential component of biological processes like protein synthesis, animal growth, and plant development because it regulates the transfer of metal elements in biological bases.
Numerous attempts have been made to create new procedures for amino acid analysis as a result of the rising focus on human health, disease diagnosis, and therapy. Currently, spectroscopic, chromatographic, or electrochemical analytical methods are most frequently employed to identify and characterize amino acids. However, each method has certain disadvantages, such as the need for equipment and trained personnel, operational simplicity, analytical cost, test speed, and detection.
Based on the important distinguishing characteristics of various amino acids to date, much research has been done on optical probes using indicator-displacement tests, metal complex coordination, particular interactions between probes and amino acids, and other techniques. We further subdivided the reaction-based probes into the following groups: production of imines, Michael addition, thiazinane or thiazolidine, cleavage of sulfonate ester, cleavage of disulfide, and others. Metal complexes-displace coordination. Due to some amino acids' similarity in structure and reactivity, it is still challenging to develop sensors that can selectively and sensitively identify amino acids from one another, such as the three biological thiols Cys, Hcy, and GSH.
Specific reactions between probes and amino acids and other techniques have been extensively researched based on the significant characteristic features of diverse amino acids to date. We further divided the reaction-based probes into the following categories: metal complexes-displace coordination, imine creation, Michael addition, thiazinane or thiazolidine formation, cleavage of a sulfonate ester, cleavage of a disulfide; and others.
Colorimetric, Fluorometric, Sensor, Amino acid.