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Current Organic Chemistry

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ISSN (Print): 1385-2728
ISSN (Online): 1875-5348

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Review Article

Overview of Synthesis and Applications of Unnatural Lipophilic α-Amino Acids

Author(s): Prateek Bhamboo, Smritilekha Bera* and Dhananjoy Mondal

Volume 28, Issue 5, 2024

Published on: 05 March, 2024

Page: [390 - 403] Pages: 14

DOI: 10.2174/0113852728297799240206084937

Price: $65

Abstract

Naturally and synthetically obtained lipophilic α-amino acids exhibit diverse properties and applications in academia and industry. Unnatural hydrophobic/lipophilic amino acids lacking polarity in their side chains manifest the biologically significant structure of peptides and proteins. The hydrophobic effect of lipophilic amino acids stabilizes the structure of proteins, peptides, and enzymes during their indigenous folding-unfolding phenomena. The presence of these amino acids in the backbone of protein and peptide-derived drug delivery systems such as lysine-derived surfactants and glycodendrimers can also enhance the cell penetration of drugs of interest. Cationic poly-l-lysine dendrimers, α-amino oleic acid, and a naturally occurring cyclic heptadepsipeptide HUN-7293 are recognized as promising biomaterials for developing prodrugs and also serve as biocompatible surfactants in the food, cosmetic and pharmaceutical industries. The synthesis of unnatural lipophilic amino acids, N-lauroyl sarcosine, N-lauroyl glutamic acid, N-octylglycine, N-myristoyl glycine etc. has gained attention for preparing novel compounds for advanced academic, industrial, and societal applications. This review article discusses the applications and synthesis of hydrophobic/lipophilic α-amino acids using ester enolate Claisen rearrangement, chiral auxiliary, chiral pool, chiral catalysts, and many more relevant methodologies.

Keywords: Unnatural, polarity, lipophilic α-amino acids, pharmaceuticals, hydrophobic effect, peptides and proteins.

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