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Usage

Uses

Used in Pharmaceutical Industry:
3-FMOC-AMINO-CYCLOHEXANECARBOXYLIC ACID is used as a key intermediate in the synthesis of various pharmaceutical compounds due to its ability to facilitate the formation of peptide bonds and its compatibility with a range of chemical reactions.
Used in Agrochemical Industry:
In the agrochemical sector, 3-FMOC-AMINO-CYCLOHEXANECARBOXYLIC ACID is utilized as a component in the development of bioactive molecules, contributing to the creation of new pesticides and other agricultural chemicals.
Used in Organic Chemistry Research:
3-FMOC-AMINO-CYCLOHEXANECARBOXYLIC ACID serves as a versatile reagent in organic chemistry, aiding researchers in exploring novel synthetic pathways and developing innovative chemical processes.
Used in Fine Chemicals Production:
It is employed as a building block in the production of fine chemicals, where its unique structure and functional groups are leveraged to create high-value specialty chemicals for various applications.

Upstream product

• 16636-51-4 trans-3-aminocyclohexanecarboxylic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 99-05-8 meta-aminobenzoic acid 
• 16636-51-4 (+/-)-cis-3-aminocyclohexanecarboxylic acid 

Downstream Products

• 1421678-19-4 C₈₈H₁₂₆N₂₀O₂₄ 

Relevant academic research and scientific papers

Introduction of cyclically constrained γ-residues stabilizes an α-peptide hairpin in aqueous solution

The synthesis and structural characterization of hybrid α/γ-peptides resulting from a 1:1 α→γ residue substitution at cross-strand positions in a hairpin-forming α-peptide sequence are described. Cyclically constrained γ-residues based on 1,3-substituted

Diaminopropionic acid derivatives

A compound of formula 1a which is useful for treating reperfusion injury, and salts, prodrugs, and related compounds.

Opioid deltorphin C analogues containing cis- or trans-2- or 3- or 4- aminocyclohexanecarboxylic acid residues

The solid phase synthesis, based on the Fmoc chemical protocol, was used to prepare ten deltorphin C (Del-C; H-Tyr-D-Ala-Phe-Asp-Val-Val-Gly-NH2) analogues containing cis- and trans- 2 or 3- or 4- aminocyclohexanecarboxylic acid (ACCA) residues at position 2, ACCA-peptides showed high resistance to degradation by plasma or brain enzymes, negligible affinity for the κ- binding site and modest δ- and/or μ-receptor affinities. Both [cis-3- ACCA2]Del-C analogues and one trans isomer are the only deltorphin analogues of this series exhibiting an appreciable δ-affinity and selectivity. These data suggest that the presence of a conformationally constrained ACCA residue in position 2 of the 'message' sequence of deltorphin C is slightly tolerated.