110990-08-4

Usage

Uses

Used in Pharmaceutical Industry:
FMOC-D-LYS-OH is used as a protecting group in solid-phase peptide synthesis for the amine functionality of lysine. This allows for selective deprotection and subsequent peptide bond formation, facilitating the synthesis of complex peptide-based drugs and bioactive molecules.
Used in Chemical Synthesis:
FMOC-D-LYS-OH is used as a building block in the synthesis of various peptide-based drugs and bioactive molecules. Its unique structure and reactivity enable the creation of diverse and potent therapeutic agents with specific biological activities.
Used in Research and Development:
FMOC-D-LYS-OH is utilized in research and development for the exploration of novel peptide-based therapeutics and the optimization of existing peptide synthesis methods. Its versatility and compatibility with various synthetic strategies make it a valuable tool for advancing the field of peptide chemistry and drug discovery.

InChI:InChI=1/C21H24N2O4.ClH/c22-12-6-5-11-19(20(24)25)23-21(26)27-13-18-16-9-3-1-7-14(16)15-8-2-4-10-17(15)18;/h1-4,7-10,18-19H,5-6,11-13,22H2,(H,23,26)(H,24,25);1H/t19-;/m1./s1

Upstream product

• 92122-45-7 Fmoc-D-Lys(BOC)-OH 

Downstream Products

• 269061-41-8 C₂₇H₂₆N₄O₈ 

Relevant academic research and scientific papers

The isolation of secondary metabolites from Rheum ribes L. and the synthesis of new semi-synthetic anthraquinones: Isolation, synthesis and biological activity

Rheum ribes L. (Rhubarb) is one of the most important edible medicinal plants in the Eastern Anatolia region and is called “I?k?n” by local people. Resveratrol and 6-O-methylalaternin were isolated from the Rhubarb for the first time in addition to well-k

Supported Catalytically Active Supramolecular Hydrogels for Continuous Flow Chemistry

Inspired by biology, one current goal in supramolecular chemistry is to control the emergence of new functionalities arising from the self-assembly of molecules. In particular, some peptides can self-assemble and generate exceptionally catalytically active fibrous networks able to underpin hydrogels. Unfortunately, the mechanical fragility of these materials is incompatible with process developments, relaying this exciting field to academic curiosity. Here, we show that this drawback can be circumvented by enzyme-assisted self-assembly of peptides initiated at the walls of a supporting porous material. We applied this strategy to grow an esterase-like catalytically active supramolecular hydrogel (CASH) in an open-cell polymer foam, filling the whole interior space. Our supported CASH material is highly efficient towards inactivated esters and enables the kinetic resolution of racemates. This hybrid material is robust enough to be used in continuous flow reactors, and is reusable and stable over months.

Fluorescent Mu selective opioid ligands from a mixture based cyclic peptide library

A positional scanning cyclic peptide library was generated using a penta-peptide thioester scaffold. Glycine was fixed at position R1. Diaminopropionic acid was fixed at position R3, with its γ-amino attaching to an anthraniloyl group. Positions R2 and R4 contained 36 l- and d- amino acids and position R5 contained 19 l- amino acids. Cyclization was performed in a mixture of acetonitrile and 1.5 M aqueous imidazole solution (7:1 v/v) at room temperature for 5 days. No significant cross-oligomerization was detected under the cyclization conditions. The library was screened in a binding assay for mu opioid receptor, identifying the active amino acid mixture at each position. A total of 40 individual cyclic peptides were identified and synthesized by the combinations of the most active amino acid mixtures found at three positions 5 × 4 × 2. Two cyclic peptides exhibited high binding affinities to opioid receptor. The most active cyclic peptide in the library was yielded to have Tyr at R2, d-Lys at R4, and Tyr at R5. Further investigation on this compound revealed the side chain-to-tail isomer to have greater binding affinity (14 nM) than the head-to-tail isomer (39 nM). Both isomers were selective for the mu-opioid receptor.