Fmoc-(R)-2-(7-octenyl)Ala-OH

Fmoc-(R)-2-(7-octenyl) Ala-OH is an unnatural Fmoc-protected amino acid and modification module. Fmoc-(R)-2-(7-octenyl) Ala-OH serves as a key building block for all-hydrocarbon cross-linking modification of antimicrobial peptides, and facilitates the generation of stapled peptide derivatives. When introduced into specific sites of the parent peptide, Fmoc-(R)-2-(7-octenyl) Ala-OH effectively increases the α-helix content of the peptide chain, thereby significantly enhancing its antimicrobial activity and proteolytic stability. Fmoc-(R)-2-(7-octenyl) Ala-OH is widely used in research on bacterial infections and the development of related antimicrobial agents^[1][2]. Stapled peptide is a specially chemically modified polypeptide. It locks the peptide chain into a stable α-helical structure by introducing a "staple"-like chemical bridge (usually an all-carbon backbone) at specific positions of the peptide chain.
In Vitro:Fmoc-(R)-2-(7-octenyl)Ala-OH (25 μM; up to 12 h) has a degradation half-life of 0.57 h in α-chymotrypsin at 37°C and is completely degraded after 12 h of incubation when incorporated into A4K14-citropin 1.1-Sp6^[1].
Fmoc-(R)-2-(7-octenyl)Ala-OH (0.39-50 μM; 96 h) inhibits the viability of C4-2B, A549, U87, and MCF-7 cells with IC₅₀ values of 35.84 μM, 30.19 μM, 34.49 μM, and 23.78 μM, respectively, when incorporated into A4K14-citropin 1.1-Sp6^[1].
Fmoc-(R)-2-(7-octenyl)Ala-OH (Fmoc-R8-OH) (18-20 h) incorporated into stapled Figainin 2 derivatives exhibit antimicrobial activity with MIC values of 9.3-18.7 μg/mL against Acinetobacter baumannii, and 37.5 μg/mL against Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli^[2].