1354752-75-2

Usage

Uses

Used in Peptide Synthesis:
(S)-2-[((9H-fluoren-9-yl)methoxy)carbonyl]amino-3-(prop-2-yn-1-yloxy)propanoic acid is used as a protected amino acid building block for the synthesis of peptides. The Fmoc group protects the amine group, preventing unwanted side reactions during the assembly of peptide chains, while the POM group shields the hydroxyl group of serine or threonine, ensuring the correct formation of peptide bonds.
Used in Drug Development:
In the pharmaceutical industry, (S)-2-[((9H-fluoren-9-yl)methoxy)carbonyl]amino-3-(prop-2-yn-1-yloxy)propanoic acid is used as a key intermediate in the development of peptide-based drugs. Its ability to protect specific functional groups allows for the precise synthesis of complex peptide structures, which can be further modified for targeted drug delivery or enhanced bioactivity.
Used in Biochemical Research:
(S)-2-[((9H-fluoren-9-yl)methoxy)carbonyl]amino-3-(prop-2-yn-1-yloxy)propanoic acid is employed as a research tool in biochemical studies, where the controlled synthesis of peptides and other biomolecules is necessary. Its protective groups enable the exploration of novel peptide sequences and their interactions with biological targets, contributing to a deeper understanding of molecular recognition and signaling pathways.
Used in Chemical Synthesis:
In the field of chemical synthesis, (S)-2-[((9H-fluoren-9-yl)methoxy)carbonyl]amino-3-(prop-2-yn-1-yloxy)propanoic acid is utilized as a versatile building block for the creation of complex organic molecules. Its protective groups facilitate the stepwise assembly of multifunctional compounds, which can be found in various applications, such as pharmaceuticals, agrochemicals, and materials science.

Upstream product

• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 145205-94-3 (S)-2-[(tert-butoxycarbonyl)amino]-3-(prop-2-yn-1-yloxy)propanoic acid 
• 675585-14-5 N-[(1,1-dimethylethoxy)carbonyl]-O-(prop-2-yn-1-yl)serine methyl ester 
• 1379150-93-2 O-propargyl-L-serine hydrochloride 
• 497-19-8 sodium carbonate 

Downstream Products

• 1558028-97-9 C₃₈H₅₅N₁₁O₁₁ 
• 1558028-92-4 C₃₂H₄₄N₈O₆ 

Relevant academic research and scientific papers

Drug Design Inspired by Nature: Crystallographic Detection of an Auto-Tailored Protease Inhibitor Template

De novo drug discovery is still a challenge in the search for potent and selective modulators of therapeutically relevant target proteins. Here, we disclose the unexpected discovery of a peptidic ligand 1 by X-ray crystallography, which was auto-tailored by the therapeutic target MMP-13 through partial self-degradation and subsequent structure-based optimization to a highly potent and selective β-sheet peptidomimetic inhibitor derived from the endogenous tissue inhibitors of metalloproteinases (TIMPs). The incorporation of non-proteinogenic amino acids in combination with a cyclization strategy proved to be key for the de novo design of TIMP peptidomimetics. The optimized cyclic peptide 4 (ZHAWOC7726) is membrane permeable with an IC50 of 21 nm for MMP-13 and an attractive selectivity profile with respect to a polypharmacology approach including the anticancer targets MMP-2 (IC50: 170 nm) and MMP-9 (IC50: 140 nm).

MACROCYCLIC COMPOUNDS

The present invention relates to macrocyclic compounds which are capable of selective binding to a target saccharide (e.g. glucose), making them particularly well suited for use in saccharide sensing applications. The present invention also relates to processes for the preparation of said compounds, to compositions and devices comprising them, and to their use in the detection of a target saccharide.

Hierarchical supramolecular hydrogels: Self-assembly by peptides and photo-controlled release: Via host-guest interaction

A hierarchical supramolecular hydrogel was self-assembled from a Fmoc-RGDS tetrapeptide and showed photo-controlled release directed by host-guest interaction. Multiple payloads, including vesicles, were successively released from a single peptide hydrogel.

Incorporation of 'click' chemistry glycomimetics dramatically alters triple-helix stability in an adiponectin model peptide

Adiponectin (Adpn) has been shown to be a possible therapeutic for Type II diabetes, however the production of a therapeutic version of Adpn has proved to be challenging. Biological studies have highlighted the importance of the glycosylated lysine residues for the formation of bioactive high molecular weight oligomers of Adpn. Through the use of 'click' glycopeptide mimetics, we investigated the role of glycosylated lysine and serine residues for the formation of triple helical structures of the collagenous domain of Adpn, in the context of a collagen model peptide scaffold. The physical properties of the unglycosylated lysine and serine peptides are compared with their glycosylated analogues. Our results highlight the crucial role of lysine residues for formation of the triple helical structure of Adpn, possibly due to the extension of both intra- and interstrand hydrogen bonding networks. Strikingly, we observed a significant decrease in thermal stability upon incorporation of triazole-linked analogues of glycosylated lysine residues into the adiponectin collageneous domain, indicating possible uses of 'click' glycomimetics for bioengineering applications.

Oxidative α,ω-diyne coupling as an approach towards novel peptidic macrocycles

The Glaser-Hay diyne coupling proved to be an efficient cyclisation approach towards diyne containing peptidic macrocycles. A variety of tetrapeptide-based macrocyclic 1,3-diynes were obtained from O-propargylated serine or tyrosine residues using Cu(OAc)2·H2O and NiCl2 under an O2-atmosphere. The effect of the linear 1,3-diyne on peptide conformations was studied by NMR and compared with a macrocycle bearing a saturated linker.

In vitro membrane permeation studies and in vivo antinociception of glycosylated Dmt1-DALDA analogues

In this study the μ opioid receptor (MOR) ligands DALDA (Tyr-d-Arg-Phe-Lys-NH2) and Dmt1-DALDA (Dmt-d-Arg-Phe-Lys-NH2, Dmt = 2′,6′-dimethyltyrosine) were glycosylated at the N- or C-terminus. Subsequently, the modified pep

Azide- and alkyne-functionalised α- And β3-amino acids

The synthesis and full characterisation of bifunctional β3-amino acids that have side chains functionalised with terminal azides (S)-4 and (R)-4 or acetylenes 5 and 6 is reported for the first time. The building blocks incorporate a turn-inducing β3-segment and a side chain that can be functionalised further, for example, through copper-catalysed Huisgen cycloaddition. Moreover, the corresponding α-amino acids 1 and 3 have been synthesised and characterised. All amino acid building blocks were of high optical purity as demonstrated by derivatisation and subsequent NMR analysis.

Azide- and alkyne-functionalised α- And β3-amino acids

The synthesis and full characterisation of bifunctional β3-amino acids that have side chains functionalised with terminal azides (S)-4 and (R)-4 or acetylenes 5 and 6 is reported for the first time. The building blocks incorporate a turn-inducing β3-segment and a side chain that can be functionalised further, for example, through copper-catalysed Huisgen cycloaddition. Moreover, the corresponding α-amino acids 1 and 3 have been synthesised and characterised. All amino acid building blocks were of high optical purity as demonstrated by derivatisation and subsequent NMR analysis. Georg Thieme Verlag KG Stuttgart · New York.