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Usage

Uses

Used in Pharmaceutical Industry:
Hexadecanoic acid, 2-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-, (S)is used as a protective group in peptide synthesis for the development of peptide-based drugs. Its role in protecting amino acids during the synthesis process ensures the stability and proper formation of peptide bonds, which is essential for creating effective and potent pharmaceutical compounds.
Used in Biomedical Research:
In the field of biomedical research, Hexadecanoic acid, 2-[[(9H-fluoren-9-ylmethoxy)carbonyl]amino]-, (S)is utilized for the synthesis of peptides that can be used in studying various biological processes and mechanisms. Its protective properties allow for the creation of peptides with specific functionalities, enabling researchers to investigate their interactions with biological systems and develop a deeper understanding of their potential applications in medicine and healthcare.

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 98393-17-0 L-2-aminohexadecanoic acid 
• 478706-42-2 tert-butyl(2S)-2-{[(1R,2R,5R)-2-hydroxy-2,6,6-trimethylbicyclo-[3.1.1]hept-3-ylidene]amino}hexadecanoate 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 478706-48-8 tert-butyl L-2-[(9-fluorenylmethoxycarbonyl)amino]hexadecanoate 

Relevant academic research and scientific papers

Diastereoselective alkylation of schiff bases for the synthesis of lipidic unnatural Fmoc-protected α-amino acids

Peptides with increased lipophilicity can cross cell membranes more easily and have longer half -life times. For these reasons, the synthesis of enantiomerically pure Fmoc-protected lipidic α-amino acids is a relevant goal. Schiff bases originating from the reaction between the two enantiomers of 2-hydroxypinan-3-one with Gly-OtBu were alkylated with a series of long alkyl halides. Diastereomeric excesses were determined by reversed-phase HPLC, under conditions carefully chosen for such lipophilic substrates. Wiley-VCH Verlag GmbH, 69451 Weinheim, Germany, 2002.

97. Synthesis of Unnatural Lipophilic N-(9H-Fluoren-9-ylmethoxy)carbonyl-Substituted α-Amino Acids and Their Incorporation into Cyclic RGD-Peptides: A Structure-Activity Study

The ανβ3 integrin is implicated in human tumor metastasis and angiogenesis. It has been shown that structures of the sequence cyclo(-Arg1-Gly2-Asp3-D-Phe 4-Xaa5-) (I) and cyclo(-Arg1-Gly2-Asp3-Phe 4-D-Xaa5-) (II) bind with high affinity and the latter with high selectivity to this receptor. The residues Xaa and D-Xaa accept a broad variety of amino acids. Here, we report on the synthesis, activities, and conformational analysis of cyclic Arg-Gly-Asp (RGD) peptides containing lipophilic amino acids Xaa or D-Xaa in position 5. For I, these were (2S)-2-aminohexadecanoic acid (Ahd) and N-hexadecylglycine (Hd-Gly) and in II, D-Ahd and Hd-Gly, and, for control purposes, Ahd were incorporated (Fig. 1). The enantiomerically pure α-amino acids were obtained by non-enantioselective synthesis and subsequent enzymatic separation of isomers using acylase I (Scheme). Hd-Gly was prepared in a modified procedure according to Stewart from ethyl bromoacetate and hexadecylamine (Scheme). The synthesis and physicochemical properties of the corresponding (9H-fluoren-9-ylmethoxy)carbonyl (Fmoc) derivatives, compatible with solid-phase peptide synthesis, are described. Structure elucidation by NMR reveals that the lipid modification has no significant impact on the template structures when incorporated into them. For peptides I with Xaa = Ahd or Hd-Gly (1 or 2), a βII′/γ-turn-like arrangement with D-Phe in i + 1 position of the β-turn is found. Peptides II with D-Xaa = D-Ahd or Hd-Gly (3 or 4) exhibit a βII′/γ-turn conformation with Gly in i + 1 position of the β-turn, whereas II with Ahd instead of D-Xaa, i.e., lacking a D-amino acid in position 4 or 5 (5), adopts no defined conformation. However, in assays of receptor specificity employing human ανβ3 integrin, the compounds exhibit IC50 values ranging from nanomolar to less than millimolar. These results indicate that although the arrangement of the pharmacophoric groups is preserved in the target compounds, the biological activity is highly dependent on spatial requirements of the lipid anchor in the receptor binding pocket. Obviously, only certain positions do not affect the binding.