84889-09-8

Usage

Uses

Used in Pharmaceutical and Biochemical Research:
FMOC-PHE-PHE-OH is utilized as a research tool for the development of novel peptides and peptidomimetics. Its role is pivotal in the synthesis of complex peptide structures, which are essential for understanding protein functions and developing new therapeutic agents.
Used in Peptide Synthesis:
In the field of organic chemistry, FMOC-PHE-PHE-OH is employed as a key building block in the synthesis of larger peptides. The protecting group ensures that the N-terminus remains unreactive until the desired point in the synthesis process, allowing for precise control over peptide assembly.
Used in Drug Development:
FMOC-PHE-PHE-OH contributes to the advancement of drug development by providing a stable and protected intermediate in the synthesis of bioactive peptides. These peptides can be further modified or used as templates for the creation of new drugs with specific therapeutic targets.
Used in Chemical Education:
FMOC-PHE-PHE-OH also serves as an educational tool in teaching the principles of peptide chemistry, synthesis strategies, and the importance of protecting groups in organic synthesis to students and researchers in chemistry and biochemistry.

Upstream product

• 63-91-2 L-phenylalanine 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-30-5 Fmoc-Phe-ONp 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 1370440-28-0 N-(((9H-fluoren-9-yl)methoxy)carbonyloxy)-2-amino-2-oxoacetimidoyl cyanide 
• 101214-43-1 Fmoc-Phe-ONSu 
• 1586761-17-2 Fmoc-Phe-Phe-O^tBu 
• 15100-75-1 L-phenylalanine tert-butyl ester hydrochloride 
• 84890-98-2 Fmoc-Phe-O-COO-isoBu 
• 126727-04-6 2-(9-fluorenylmethoxycarbonylamino)-3-phenylpropionic acid 
• 474316-98-8 Fmoc-Phe-Phe-NHNHPh 

Downstream Products

• 1426326-90-0 C₈₇H₁₂₉N₃O₈ 
• 79396-84-2 Fmoc-Phe-Leu-OH 

Relevant academic research and scientific papers

Two approaches for the engineering of homogeneous small-molecule hydrogels

Small-molecule hydrogelators have been widely used to engineer supramolecular hydrogels for biomedical applications. Typically, a change of the solubility of small molecules in solvent is used to trigger the gelation process. This requires a switch of pH or solvent by mixing two different types of solutions. However, due to the intrinsic ragged free energy landscape that underlies the self-assembly process and the high viscosity of the solution that limits the diffusion, the hydrogels made by these methods are often limited by their inhomogeneity and irreproducible physical properties. It is therefore desirable to circumvent these drawbacks and produce homogeneous hydrogels. Conversely, only a few studies have been done towards this direction. In this article, we present two novel approaches to engineer homogeneous hydrogels. One is based on the nano-dispersed colloids to hydrogel transition and the other is based on the decomposition of potassium persulfate to mildly change the pH. These two methods allow kinetically controlling the self-assembly process and the resulting hydrogels are indeed more homogeneous and reproducible. Moreover, the structural and morphological characterizations suggest that the structures of the hydrogels prepared by different approaches are distinct from each other, leading to diverse macroscopic mechanical properties. These results suggest that besides the thermodynamics, the self-assembly kinetics also plays an important role in determining the properties of the final assembled hydrogels. We propose that it is possible to rationally tune the physical properties of the hydrogels by simply control the self-assembly kinetics without changing the structure of the small-molecule hydrogelators.

Self-Assembled Peptide-Based Hydrogels as Scaffolds for Proliferation and Multi-Differentiation of Mesenchymal Stem Cells

Fluorenyl-9-methoxycarbonyl (Fmoc)-diphenylalanine (Fmoc-FF) and Fmoc-arginine-glycine--aspartate (Fmoc-RGD) peptides self-assemble to form a 3D network of supramolecular hydrogel (Fmoc-FF/Fmoc-RGD), which provides a nanofibrous network that uniquely presents bioactive ligands at the fiber surface for cell attachment. In the present study, mesenchymal stem cells (MSCs) in Fmoc-FF/Fmoc-RGD hydrogel increase in proliferation and survival compared to those in Fmoc-FF/Fmoc-RGE hydrogel. Moreover, MSCs encapsulated in Fmoc-FF/Fmoc-RGD hydrogel and induced in each defined induction medium undergo in vitro osteogenic, adipogenic, and chondrogenic differentiation. For in vivo differentiation, MSCs encapsulated in hydrogel are induced in each defined medium for one week, followed by injection into gelatin sponges and transplantation into immunodeficient mice for four weeks. MSCs in Fmoc-FF/Fmoc-RGD hydrogel increase in differentiation into osteogenic, adipogenic, and chondrogenic differentiation, compared to those in Fmoc-FF/Fmoc-RGE hydrogel. This study concludes that nanofibers formed by the self-assembly of Fmoc-FF and Fmoc-RGD are suitable for the attachment, proliferation, and multi-differentiation of MSCs, and can be applied in musculoskeletal tissue engineering. (Figure presented.).

Benzoisothiazolone (BIT): A Fast, Efficient, and Recyclable Redox Reagent for Solid Phase Peptide Synthesis

Solid-phase peptide synthesis (SPPS), a preferred synthetic procedure, generates by-products and effluents in multiple equivalents for one equivalent of desired product. Presented herein is the use of a fast and efficient coupling protocol for SPPS using a benzoisothiazolone (BIT), which can be fully recycled. The BIT, as redox activator, works under very mild conditions and generates minimal amount of waste. As a case study, the BIT coupling protocol is applied to the synthesis of side chain of the recently discovered antibiotic, teixobactin.

A catalytic one-step synthesis of peptide thioacids: the synthesis of leuprorelin via iterative peptide-fragment coupling reactions

A catalytic one-step synthesis of peptide thioacids was developed. The oxygen-sulfur atom exchange reaction converted the carboxy group at the C-terminus of the peptides into a thiocarboxy group with suppressed epimerization. This method was successfully applied to the synthesis of the peptide drug leuprorelin via an iterative fragment-coupling protocol.

Regulating Higher-Order Organization through the Synergy of Two Self-Sorted Assemblies

The extracellular matrix (ECM) is the natural fibrous scaffold that regulates cell behavior in a hierarchical manner. By mimicking the dynamic and reciprocal interactions between ECM and cells, higher-order molecular self-assembly (SA), mediated through the dynamic growth of scaffold-like nanostructures assembled by different molecular components, was developed. Designed and synthesized were two self-sorted coumarin-based gelators, a peptide molecule and a benzoate molecule, which self-assemble into nanofibers and nanobelts, respectively, with different dynamic profiles. Upon the dynamic growth of the fibrous scaffold assembled from peptide gelators, nanobelts assembled from benzoate gelators transform into a layer-by-layer nanosheet, reaching ninefold increase in height. By using light and an enzyme, the spatial–temporal growth of the scaffold can be modified, leading to in situ height regulation of the higher-order architecture.

Hydrogel composition for carbon monoxide release and preparation method thereof

The present invention relates to a hydrogel composition for carbon monoxide release, which contains a gellant and a co-magnetic assembly of a carbon monoxide releasing molecule bound to a peptide, and to a manufacturing method thereof. The synthesized carbon monoxide releasing hydrogel (CORH) according to the present invention has excellent mechanical properties, exhibits excellent effects on damage due to oxidative stress, and has characteristics of being gradually released in the body, and thus it is possible to obtain an effect of protecting myocardial cells and reducing cell death through proper release of the carbon monoxide, thereby being expected to be widely used as a therapeutic agent.COPYRIGHT KIPO 2018

Fmoc-Amox, A Suitable Reagent for the Introduction of Fmoc

Synthesis of most peptides is achieved using solid-phase peptide synthesis employing the Fmoc/tert-butyl strategy. However, the introduction of Fmoc in N-unprotected amino acids seems to be challenging due to the formation of dipeptides and sometimes tripeptides as impurities and β-alanyl impurities when Fmoc-OSu is used as well. Herein, we report an efficient and successful method using Fmoc-Amox, which is an oxime based derivative, toward the synthesis of Fmoc-glycine with no traces of side reactions. Fmoc-Amox is inexpensive, and Amox can be easily removed after the reaction, thus affording pure Fmoc-Gly-OH devoid of any detrimental impurities or contamination, mainly dipeptide or Amox itself, as shown by high-performance liquid chromatography and NMR, respectively.

Facile synthesis of a peptidic Au(i)-metalloamphiphile and its self-assembly into luminescent micelles in water

We report a short synthetic route for the preparation of a peptidic Au(i)-metalloamphiphile which, in buffered environments of physiological ionic strength, self-assembles into luminescent micellar nanostructures of 14 nm in diameter. This journal is

Photodegradation of amyloid β and reduction of its cytotoxicity to PC12 cells using porphyrin derivatives

A purpose-designed porphyrin-peptide hybrid effectively degraded amyloid β monomer and oligomers associated with Alzheimer's disease. Degradation was achieved using light irradiation in the absence of any additives and under neutral conditions. Moreover,

α-N-Protected dipeptide acids: A simple and efficient synthesis via the easily accessible mixed anhydride method using free amino acids in DMSO and tetrabutylammonium hydroxide

The importance of dipeptides both in medicinal and pharmacological fields is well documented and many efforts have been made to find simple and efficient methods for their synthesis. For this reason, we have investigated the synthesis of α-N-protected dipeptide acids by reacting the easily accessible mixed anhydride of α-N-protected amino acids with free amino acids under different reaction conditions. The combination of TBA-OH and DMSO has been found to be the best to overcome the low solubility of amino acids in organic solvents. Under these experimental conditions, the homogeneous phase condensation reaction occurs rapidly and without detectable epimerization. The present method is also applicable to side-chain unprotected Tyr, Trp, Glu, and Asp but not Lys. This latter residue is able to engage two molecules of mixed anhydride giving the corresponding isotripeptide. Moreover, the applicability of this protocol for the synthesis of tri- and tetrapeptides has been tested. This approach reduces the need for protecting groups, is cost effective, scalable, and yields dipeptide acids that can be used as building blocks in the synthesis of larger peptides.