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Fmoc-β-alanine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Fmoc-β-alanine is an amino acid building block used in peptide synthesis. With a growing peptide drug market the fast, reliable synthesis of peptides is of great importance.

Category

Fmoc-Amino Acids

Catalog number

BAT-007586

CAS number

35737-10-1

Molecular Formula

C18H17NO4

Molecular Weight

311.30

IUPAC Name

3-(9H-fluoren-9-ylmethoxycarbonylamino)propanoic acid

Synonyms

Fmoc-β-Ala-OH; 3-Fmoc-aminopropanoic acid; N-(9-Fluorenylmethoxycarbonyl)-β-alanine; N-Fluorenylmethoxycarbonyl-β-alanine; 3-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)propanoic Acid; 3-(9-Fluorenylmethoxycarbonylamino)propionic Acid; 3-[[[(9H-Fluoren-9-yl)methoxy]carbonyl]amino]propionic Acid; Fmoc-beta-alanine; Fmoc-beta-Ala-OH; FMOC-b-Ala-OH; n-fmoc-beta-alanine; Fmoc-b-Alanine; Fmoc beta Ala OH

Appearance

White powder

Purity

≥ 99% (HPLC)

Density

1.284 g/cm3

Melting Point

145-150 °C

Boiling Point

555.8 °C at 760 mmHg

Storage

Store at 2-8 °C

InChI

InChI=1S/C18H17NO4/c20-17(21)9-10-19-18(22)23-11-16-14-7-3-1-5-12(14)13-6-2-4-8-15(13)16/h1-8,16H,9-11H2,(H,19,22)(H,20,21)

InChI Key

LINBWYYLPWJQHE-UHFFFAOYSA-N

Canonical SMILES

C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)NCCC(=O)O

Fmoc-β-alanine, a chemical compound with diverse applications in peptide synthesis and biomedical fields, exhibits a wide range of uses. Here are the key applications, presented with high perplexity and burstiness:

Peptide Synthesis: Serving as a foundational element in solid-phase peptide synthesis, Fmoc-β-alanine plays a crucial role in incorporating β-amino acids into peptide chains, thereby enhancing the stability and functionality of the resulting peptides. This technique is vital for the creation of peptide-based drugs and biomaterials with specific properties, pushing the boundaries of therapeutic development towards precision medicine.

Drug Development: In the dynamic landscape of pharmaceutical research, Fmoc-β-alanine acts as a linchpin for designing and producing innovative bioactive peptides and peptide mimetics. By integrating β-alanine into peptide sequences, researchers can magnify the binding affinity, selectivity, and stability of potential therapeutic agents, paving the way for groundbreaking treatments in areas such as cancer, diabetes, and infectious diseases, reshaping the future of medicine.

Proteomics: Embracing the realm of protein interactions and functions, Fmoc-β-alanine emerges as a valuable tool for scientists. Through the synthesis of peptide probes containing β-alanine, researchers gain insights into protein conformations, binding sites, and signaling pathways, unraveling the intricacies of cellular processes and unearthing novel drug targets, heralding a new era of targeted therapeutics and precision medicine.

Nanotechnology: Fmoc-β-alanine finds application in the intricate world of peptide-based nanomaterials, where its unique chemical properties enable the fabrication of self-assembling nanostructures with diverse functions. By harnessing these capabilities, researchers craft nanomaterials for drug delivery, tissue engineering, and biosensing, offering tantalizing prospects like targeted delivery, controlled release, and biocompatibility, shaping the landscape of nanomedicine and regenerative technologies.

1.Formation of Fmoc-beta-alanine during Fmoc-protections with Fmoc-OSu.

Obkircher M1, Stähelin C, Dick F. J Pept Sci. 2008 Jun;14(6):763-6. doi: 10.1002/psc.1001.

During the Fmoc-protection of H-alpha-Me-Val-OH, an unknown side product was found and isolated. The characterization using various analytical methods led unambiguously to the result that Fmoc-beta-Ala-OH was formed during the reaction. The reagent Fmoc-OSu was proven to be the source of Fmoc-beta-Ala-OH, following a mechanism that involved many deprotonation and elimination steps and a Lossen-type rearrangement as key sequence. The impurity Fmoc-beta-Ala-OH was found in a variety of reactions in which Fmoc-OSu was applied, either in the reaction mixture or as a contamination of the crude product. Purification of the Fmoc-amino acid derivatives from this impurity incurred high costs and significant reductions in yield.

2.Studies on a Dithiane-Protected Benzoin Photolabile Safety Catch Linker for Solid-Phase Synthesis.

Lee HB1, Balasubramanian S. J Org Chem. 1999 May 14;64(10):3454-3460.

Substituted benzoinyl systems 8a-g, differing either in the substitution pattern, type of resin matrix used, or resin loading capacity, were prepared and the kinetics of their photolytic cleavage of Fmoc-beta-alanine examined on resin. The linker systems 6a-g were assembled in near-quantitative yield using Corey-Seebach dithiane addition. The dithiane group that serves as a safety catch against premature photoreaction was removed by either oxidation or alkylation. Analytical methods that include FTIR and (13)C gel-phase NMR spectroscopy were used for rapid reaction monitoring and sample characterization on resin. A survey of different substituted systems 8c-f for releasing Fmoc-beta-alanine confirmed that the 3-alkoxybenzoin linker photocleaves most rapidly to give the highest yield (tau(1/2) = 6.7 min; 98% yield). Lowering the resin loading from 0.59 mmol/g in 8a to 0.26 mmol/g in 8b improved the cleavage kinetics to tau(1/2) = 2.6 min, 92% yield.

3.Multipin peptide synthesis at the micromole scale using 2-hydroxyethyl methacrylate grafted polyethylene supports.

Valerio RM1, Bray AM, Campbell RA, Dipasquale A, Margellis C, Rodda SJ, Geysen HM, Maeji NJ. Int J Pept Protein Res. 1993 Jul;42(1):1-9.

The multipin peptide synthesis procedure has been adapted to allow the synthesis of peptides at micromole loadings. The original solid pin support was replaced with a detachable crown-shaped polyethylene support with an increased surface area. In addition, the polyethylene crowns were radiation-grafted with 2-hydroxyethyl methacrylate monomer instead of acrylic acid to yield hydroxy functionalized supports with a larger concentration of polymer and hence a larger peptide capacity. Fmoc-beta-Alanine was directly esterified to the HEMA hydroxy groups with subsequent addition of a diketopiperazine-forming handle for peptide attachment. Peptides varying in length from 10 to 25 residues were assembled at a number of loadings from 1.0 to 2.2 mumol. Purity of peptides at all loadings was equal to, and in some instances superior to, that achieved on conventional solid-phase supports.

4.Tuning the self-assembly of the bioactive dipeptide L-carnosine by incorporation of a bulky aromatic substituent.

Castelletto V1, Cheng G, Greenland BW, Hamley IW, Harris PJ. Langmuir. 2011 Mar 15;27(6):2980-8. doi: 10.1021/la104495g. Epub 2011 Feb 21.

The dipeptide L-carnosine has a number of important biological properties. Here, we explore the effect of attachment of a bulky hydrophobic aromatic unit, Fmoc [N-(fluorenyl-9-methoxycarbonyl)] on the self-assembly of Fmoc-L-carnosine, i.e., Fmoc-β-alanine-histidine (Fmoc-βAH). It is shown that Fmoc-βAH forms well-defined amyloid fibrils containing β sheets above a critical aggregation concentration, which is determined from pyrene and ThT fluorescence experiments. Twisted fibrils were imaged by cryogenic transmission electron microscopy. The zinc-binding properties of Fmoc-βAH were investigated by FTIR and Raman spectroscopy since the formation of metal ion complexes with the histidine residue in carnosine is well-known, and important to its biological roles. Observed changes in the spectra may reflect differences in the packing of the Fmoc-dipeptides due to electrostatic interactions. Cryo-TEM shows that this leads to changes in the fibril morphology.