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Fmoc-L-alanine N-hydroxysuccinimide ester

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

Category

Fmoc-Amino Acids

Catalog number

BAT-003731

CAS number

73724-40-0

Molecular Formula

C22H20N2O6

Molecular Weight

408.40

Fmoc-L-alanine N-hydroxysuccinimide ester

IUPAC Name

(2,5-dioxopyrrolidin-1-yl) (2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoate

Synonyms

Fmoc-L-Ala-OSu; N-(fluorenyl-9-methoxycarbonyl)-L-alanine N-fmoc-L-alanine N-hydroxysuccinimide ester; Fmoc-Ala-OSu

Appearance

White to off-white powder

Purity

≥ 98% (HPLC)

Density

1.40±0.1 g/cm3

Melting Point

158-164 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C22H20N2O6/c1-13(21(27)30-24-19(25)10-11-20(24)26)23-22(28)29-12-18-16-8-4-2-6-14(16)15-7-3-5-9-17(15)18/h2-9,13,18H,10-12H2,1H3,(H,23,28)/t13-/m0/s1

InChI Key

FZBMNXOJLBTQHV-ZDUSSCGKSA-N

Canonical SMILES

CC(C(=O)ON1C(=O)CCC1=O)NC(=O)OCC2C3=CC=CC=C3C4=CC=CC=C24

Fmoc-L-alanine N-hydroxysuccinimide ester, a versatile chemical reagent in peptide synthesis, finds varied applications in biochemical research. Here are the key applications presented with high perplexity and burstiness:

Peptide Synthesis: In the realm of solid-phase peptide synthesis (SPPS), Fmoc-L-alanine N-hydroxysuccinimide ester stands as a cornerstone. Acting as a shielded amino acid building block, it facilitates the stepwise addition of amino acids to craft peptides. With the Fmoc group ensuring seamless deprotection, the process achieves exceptional efficiency and yield in peptide construction.

Protein Engineering: Within protein engineering endeavors, this compound assumes a pivotal role in elucidating protein structure and function using synthetic peptides. By integrating Fmoc-L-alanine derivatives into peptides, researchers delve into the repercussions of specific amino acid modifications on protein behavior. Ultimately, this methodology aids in the creation of proteins boasting enhanced stability, activity, or novel functionalities.

Drug Discovery: In the domain of drug discovery, Fmoc-L-alanine N-hydroxysuccinimide ester emerges as a key player in synthesizing peptide-based drug candidates. These peptides synthesized with the reagent mimic natural protein interactions, rendering them invaluable in the quest for new therapeutics. Researchers leverage these peptides to screen for potential drug targets and enhance lead compounds for heightened efficacy and reduced side effects.

Diagnostic Development: Beyond drug discovery, this reagent proves instrumental in crafting diagnostic assays featuring peptide probes. Synthesized peptides serve as the foundation for highly specific and sensitive assays aimed at detecting biomarkers in clinical samples. Through the use of Fmoc-L-alanine N-hydroxysuccinimide ester, scientists meticulously construct precise peptide sequences crucial for the development of accurate diagnostic tools.

1. Amine coupling through EDC/NHS: a practical approach

Marcel J E Fischer Methods Mol Biol. 2010;627:55-73. doi: 10.1007/978-1-60761-670-2_3.

Surface plasmon resonance (SPR) is one of the leading tools in biomedical research. The challenge in its use is the controlled positioning of one of the components of an interaction on a carefully designed surface. Many attempts in interaction analysis fail due to the non-functional or unsuccessful immobilization of a reactant onto the complex matrix of that surface. The most common technique for linking ligands covalently to a hydrophilic solid surface is amine coupling via reactive esters. In this chapter detailed methods and problem discussions will be given to assist in fast decision analysis to optimize immobilization and regeneration. Topics in focus are different coupling techniques for small and large molecules, streptavidin-biotin sandwich immobilization, and optimizing regeneration conditions.

2. Fmoc N-hydroxysuccinimide ester: A facile and multifunctional role in N-glycan analysis

Chang Wang, Yike Wu, Sheng Liu, Liang Zhang, Bi-Feng Liu, Xin Liu Anal Chim Acta. 2020 Sep 22;1131:56-67. doi: 10.1016/j.aca.2020.07.044. Epub 2020 Jul 30.

N-glycans that are fluorescently tagged by glycosylamine acylation have become a promising way for glycan biomarker discovery. Here, we describe a simple and rapid method using Fmoc N-hydroxysuccinimide ester (Fmoc-OSu) to label N-glycans by reacting with their corresponding intermediate glycosylamines produced by microwave-assisted deglycosylation. After optimizing reaction conditions, this derivatization reaction can be effectively achieved under 40 °C for 1 h. Moreover, the comparison of fluorescent intensities for Fmoc-OSu, Fmoc-Cl and 2-AA labeling strategies were also performed. Among which, the fluorescent intensities of Fmoc-OSu labeled glycan derivatives were approximately 5 and 13 times higher than that labeled by Fmoc-Cl and 2-AA respectively. Furthermore, the developed derivatization strategy has also been applied for analyzing serum N-glycans, aiming to screen specific biomarkers for early diagnosis of lung squamous cell cancer. More interestingly, the preparation of free reducing N-glycan standards have been achieved by the combination of HPLC fraction of Fmoc labeled glycan derivatives and Fmoc releasing chemistry. Overall, this proposed method has the potential to be used in functional glycomic study.

3. Improved detection of β-N-methylamino-L-alanine using N-hydroxysuccinimide ester of N-butylnicotinic acid for the localization of BMAA in blue mussels (Mytilus edulis)

Rudolf Andrýs, Javier Zurita, Nadezda Zguna, Klaas Verschueren, Wim M De Borggraeve, Leopold L Ilag Anal Bioanal Chem. 2015 May;407(13):3743-50. doi: 10.1007/s00216-015-8597-2. Epub 2015 Mar 28.

β-N-Methylamino-L-alanine (BMAA) is an important non-protein amino acid linked to neurodegenerative diseases, specifically amyotrophic lateral sclerosis (ALS). Because it can be transferred and bioaccumulated higher up the food chain, it poses significant public health concerns; thus, improved detection methods are of prime importance for the identification and management of these toxins. Here, we report the successful use of N-hydroxysuccinimide ester of N-butylnicotinic acid (C4-NA-NHS) for the efficient separation of BMAA from its isomers and higher sensitivity in detecting BMAA compared to the current method of choice using 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate (AQC) derivatization. Implementation of this efficient method allowed localization of BMAA in the non-visceral tissues of blue mussels, suggesting that more efficient depuration may be required to remove this toxin prior to consumption. This is a crucial method in establishing the absence or presence of the neurotoxic amino acid BMAA in food, environmental or biomedical samples.