The Importance of 6-Aminohexanoic Acid as a Hydrophobic, Flexible Structural Element

Abstract

6-aminohexanoic acid is an ω-amino acid with a hydrophobic, flexible structure. Although the ω-amino acid in question is mainly used clinically as an antifibrinolytic drug, other applications are also interesting and important. This synthetic lysine derivative, without an α-amino group, plays a significant role in chemical synthesis of modified peptides and in the polyamide synthetic fibers (nylon) industry. It is also often used as a linker in various biologically active structures. This review concentrates on the role of 6-aminohexanoic acid in the structure of various molecules.

Host-genotype-dependent cecal microbes are linked to breast muscle metabolites in Chinese chickens

“…Four of the 17 metabolites belonged to dipeptides and three of them, i.e., tyrosyl-alanine, phenylalanyl-alanine, and isoleucyl-alanine, existed in all breeds and were highly represented in the CH, RW, and Nongda Yellow A (NYA) breeds. Aminocaproic acid, a derivative of the amino acid lysine ( Markowska et al., 2021 ), exhibited the highest abundance among the 17 compounds in all chicken breeds and was also enriched in the CH, RW, and NYA breeds. This compound can only be found in the diet or the gut microbiota ( Atkinson et al., 2013 ; Xu et al., 2006 ) but not formed naturally in chickens.…”

Evaluating the In Vitro Activity and Safety of Modified LfcinB Peptides as Potential Colon Anticancer Agents: Cell Line Studies and Insect-Based Toxicity Assessments

“…This discrepancy in activity suggests distinct interaction patterns between the peptides and the two cell lines. Despite Ahx being a hydrophobic amino acid itself, in the in silico analysis, its presence in the peptide led to a decrease in overall lipophilicity, possibly due to changes in the arrangement of the molecule by changing intermolecular interactions. Nonetheless, the inclusion of Ahx is unlikely to interfere with the interaction between the peptide’s cationic charges and the cell membrane, assuming that the peptides adopt an α helical conformation (Figure A).…”

In Vitro Antifungal Activity of Chimeric Peptides Derived from Bovine Lactoferricin and Buforin II against Cryptococcus neoformans var. grubii

“…It exhibits hydrophobic behavior and has a flexible structure and adequate space between its terminal amino and carboxyl groups that give this molecule the possibility of being used as a spacer and linker of fragments of active molecules. Ahx does not necessarily generate antimicrobial activity by itself, but when conjugated with peptides, it can significantly improve antimicrobial activity [ 29 , 30 ].…”