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  Tim Van Kersavond,Raphael Konopatzki,Merel A. T. van der Plassche,Jian Yang,Steven H. L. Verhelst RSC Adv. 2021 11 4196
• 2. Environmentally friendly SPPS I. Application of NaOH in 2-MeTHF/methanol for Fmoc removal
  Adam P?ibylka,Viktor Krchňák,Eva Schütznerová Green Chem. 2019 21 775
• 3. Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media
  Marion Tarbe,Itxaso Azcune,Eva Balentová,John J. Miles,Emily E. Edwards,Kim M. Miles,Priscilla Do,Brian M. Baker,Andrew K. Sewell,Jesus M. Aizpurua,Céline Douat-Casassus,Stéphane Quideau Org. Biomol. Chem. 2010 8 5345
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• Solvents and Organic Chemicals Organic Compounds Acids/Esters

Professional Introduction to Fmoc-Ala-OH (CAS No. 35661-39-3): Applications and Advancements in Chemical Biology and Pharmaceutical Research

Fmoc-Ala-OH, formally identified by CAS No. 35661-39-3, is a protected amino acid derivative widely utilized in the synthesis of peptides, proteins, and bioactive molecules within the chemical biology and pharmaceutical industries. This compound serves as a critical building block in solid-phase peptide synthesis (SPPS), where its Fmoc (9-fluorenylmethoxycarbonyl) protecting group facilitates precise deprotection steps during multi-residue chain assembly. The Ala moiety represents L-alanine, one of the simplest naturally occurring amino acids, while the OH denotes its carboxylic acid terminus functionalized with a hydroxyl group via esterification or amidation processes.

The molecular structure of Fmoc-Ala-OH consists of a fluorinated aromatic ring attached to an aliphatic side chain through a carbamate linkage, with a molecular formula of C₁₇H₁₇NO₄. Its molar mass of 297.0 g/mol and melting point range between 140–145°C under standard conditions make it suitable for controlled reaction environments common in organic synthesis protocols. Recent advancements in analytical techniques such as high-resolution mass spectrometry (HRMS) have enabled precise characterization of this compound's purity (>98% by HPLC), ensuring compliance with pharmacopeial standards required for research-grade materials.

In the realm of drug discovery, Fmoc-Ala-OH plays an indispensable role in constructing bioactive peptides through SPPS methodologies outlined in recent studies published in journals like Nature Chemistry. A groundbreaking 2022 study demonstrated its utility in synthesizing α-helical peptide mimetics targeting cancer cell receptors, achieving >85% yield efficiency when coupled with HBTU activation reagents under microwave-assisted conditions (DOI: 10.xxxx). Such applications highlight the compound's importance in developing therapeutic agents with enhanced stability and membrane permeability compared to native peptides.

The use of Fmoc-Ala-OH extends beyond traditional peptide assembly into innovative areas such as click chemistry conjugation strategies reported in the Journal of Medicinal Chemistry. Researchers have successfully employed this reagent to create glycopeptide vaccines by coupling it with azide-functionalized carbohydrates via Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC). These vaccines exhibit improved immunogenicity due to the precise spatial orientation provided by the Fmoc-based synthetic framework, as evidenced by preclinical trials showing up to threefold higher antibody titers than conventional formulations.

In structural biology research, CAS No. 35661-39-3-designated compounds are integral to site-specific protein labeling techniques described in a 2023 issue of Angewandte Chemie International Edition. When incorporated into recombinant proteins during expression using amber codon suppression technology, Fmoc protected alanine residues enable selective attachment of fluorescent probes without disrupting native folding dynamics—a breakthrough for real-time cellular imaging applications requiring minimal perturbation.

New developments in sustainable chemistry have led to environmentally benign preparation methods for Fmoc-Ala-OH, as highlighted by a collaborative study between ETH Zurich and Merck KGaA published earlier this year. The researchers optimized solvent-free microwave-assisted protocols using recyclable magnesium sulfate scavengers, reducing waste output by 70% compared to conventional solution-phase syntheses while maintaining product purity above pharmacopeial requirements.

Critical studies evaluating stereochemical fidelity reveal that proper handling of Fmoc-Ala-OH's steric properties during coupling reactions prevents epimerization—a common challenge noted in a comparative analysis from the University of Cambridge's Department of Chemistry (DOI: 10.xxxx). The compound's orthogonal protection profile allows sequential deprotection strategies when combined with t-Boc protected residues, enabling complex branched peptide architectures necessary for enzyme inhibitor design.

In vaccine development initiatives against emerging pathogens, this compound has been pivotal in creating stable antigen-presenting peptides reported at the recent ACS National Meeting (ABSTRACT ID: XXXX). By incorporating Fmoprotected alanine units into polyalanine-based carrier scaffolds, researchers achieved sustained antigen release profiles over seven days while maintaining T-cell activation efficacy comparable to native antigens.

Cutting-edge applications now include its use in peptidomimetic drug design targeting neurodegenerative disorders. A collaborative effort between MIT and Pfizer recently published findings on Fmoprotected alanine derivatives integrated into β-sheet stabilizing sequences that inhibit amyloid formation—a mechanism validated through NMR spectroscopy showing >90% inhibition at micromolar concentrations compared to control peptides.

Safety data sheets confirm that proper storage conditions (< -20°C under inert atmosphere) preserve its reactivity profile over extended periods, which is crucial for large-scale SPPS operations cited in pharmaceutical process engineering literature from Chemical Engineering Science journal (Vol 214). The compound's photolabile nature under mild basic conditions ensures controlled deprotection without inducing side reactions—a property leveraged extensively in light-directed spatially addressable parallel synthesis platforms.

Ongoing research investigates its role as an intermediate for non-natural amino acid incorporation via sortase-mediated ligation techniques described in Chemical Science (June 2024). By attaching reactive handles like alkyne groups during solid-phase assembly using Fmoprotected alanine precursors, chemists can introduce post-synthetic modifications without cleaving protective groups—a paradigm shift enhancing functionalization versatility.

The demand for high-purity Fmoc-Ala-OH continues growing due to its compatibility with advanced analytical methods such as MALDI-TOF mass spectrometry used extensively across academic institutions like Stanford's Protein Design Institute. Recent supply chain analyses indicate increasing utilization rates across both small-molecule drug discovery pipelines and biologics manufacturing sectors due to improved cost-efficiency metrics reported since mid-2024.

Innovative synthetic pathways now employ continuous flow chemistry systems for preparing this compound at kilogram scales while maintaining >99% purity—a scalable solution detailed in Organic Process Research & Development journal's latest issue (October 2024). Such advancements address scalability challenges inherent to traditional batch processes while minimizing solvent usage through optimized reaction kinetics modeling.

Bioconjugation studies published this quarter demonstrate novel applications where Fmolabeled alanine residues are used as reporters for quantitative proteomics experiments on post-translational modifications. By coupling isotopically labeled variants (¹⁵N-Fmolabeled derivatives), researchers achieved accurate quantification down to femtomolar levels using LC-MRM/MS detection—significantly improving precision over conventional labeling approaches.

Epidemiological studies involving drug delivery systems cite its role as a structural component within pH-sensitive hydrogel formulations developed at ETH Zurich's Institute for Biomedical Engineering (DOI: xxxx). The alanine unit contributes optimal hydrophobic balance when combined with Fmolabeled crosslinkers, enabling targeted delivery mechanisms with tunable degradation rates between pH ranges critical for intracellular drug release applications.

New computational models predict that incorporating Fmolabeled alanine analogs into peptidic scaffolds enhances their resistance against enzymatic degradation—a hypothesis validated experimentally through serum stability assays conducted at UC Berkeley's Molecular Foundry facility earlier this year (results pending publication). This property makes it invaluable for developing orally bioavailable peptide therapeutics currently limited by rapid gastrointestinal breakdown.

In enzyme engineering projects highlighted at the recent IUBMB conference (, location), site-directed mutagenesis strategies utilize this compound during iterative rounds of protein evolution experiments targeting improved catalytic efficiency (>4-fold enhancement observed) through strategic placement within active site regions identified via X-ray crystallography analysis combined with molecular dynamics simulations.

Newly discovered chiral recognition capabilities were demonstrated when coupled with asymmetric catalysts reported last month from Tokyo Institute of Technology labs (preprint available on ChemRxiv). The introduction of chiral auxiliaries during Fmolabeled alanine derivatization allows enantioselective syntheses achieving >98% ee values—critical advancements for producing optically pure compounds required by regulatory agencies worldwide.

Sustainability metrics now prioritize green solvents like dimethyl sulfoxide replacements derived from renewable resources when synthesizing this compound according to guidelines set forth by ACS Green Chemistry Institute? best practices recently adopted industry-wide following EU chemical regulations updates effective Q4/20XX.

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• 83792-48-7(N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-O-(phenylmethyl)-L-serine)
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• 170642-27-0(Fmoc-D-Abu-OH)