Fmoc-D-Asp(All)-OH

Fmoc-D-Asp(All)-OH is an Fmoc-protected D-aspartic acid derivative bearing an allyl-protected side-chain carboxyl group, providing two orthogonally protected functional handles for peptide chemistry. The molecule contains a chiral α-carbon (D configuration) that supports stereochemically defined incorporation into peptide sequences, while the Fmoc group enables base-mediated N-deprotection and the allyl ester can be removed under palladium-catalyzed conditions to reveal the side-chain carboxylic acid. The presence of both a protected amino terminus and a masked side-chain acid creates a controlled reactivity profile that minimizes undesired side reactions during coupling and subsequent transformations. The free carboxylic acid at the α-position (as the amino acid acid form) and the protected side-chain functionality make it suitable for stepwise assembly of aspartate-containing peptides and for downstream derivatization into chemically defined intermediates.

1. Peptide Synthesis

Fmoc-D-Asp(All)-OH is applied in peptide building-block preparation where orthogonal protection of the α-amino function and the side-chain carboxyl group supports reliable peptide coupling chemistry. The Fmoc-protected nitrogen participates in standard peptide assembly after base-triggered Fmoc removal, while the allyl ester on the side-chain carboxyl helps suppress side-chain participation during amide bond formation. The D stereochemistry at the aspartate α-carbon enables stereodefined incorporation into peptides for studies requiring non-L aspartate residues or epimerization-resistant sequence design. Allyl deprotection can subsequently generate a free aspartate side chain for salt-bridge formation, metal coordination motifs, or further functional group transformations, aligning the compound with routine protected amino acid synthesis workflows.

2. Peptidomimetics And SAR Studies

Fmoc-D-Asp(All)-OH is utilized in peptidomimetic construction and structure-activity relationship studies that require controlled presentation of an aspartate side-chain carboxyl group. The allyl-protected side-chain carboxyl can be converted into activated acid derivatives or directly unveiled to enable conjugation, ion-binding motif tuning, or incorporation into constrained analogs where side-chain acidity governs binding interactions. The Fmoc handle supports iterative synthesis of analog libraries, while the D configuration provides stereochemical diversity for mapping receptor or enzyme recognition preferences. Downstream derivatization from the exposed aspartate acid can generate amide, ester, or mixed anhydride intermediates that feed into SAR-focused molecular design and comparative scaffold evaluation.

3. Protein Engineering Workflows

Fmoc-D-Asp(All)-OH is suitable for protein engineering and chemical protein modification workflows that rely on chemically defined aspartate residues within peptide segments. The compound's protected amino acid format supports incorporation into synthetic peptides used as ligation partners, epitope tags, or substrate/inhibitor fragments that later undergo side-chain unmasking to restore native-like acidic functionality. The orthogonal Fmoc/allyl protection strategy allows selective deprotection steps, enabling sequential functionalization without perturbing the peptide backbone. The resulting aspartate side chain can be used to introduce charge-specific interactions or to prepare peptide fragments for further conjugation chemistry, supporting downstream generation of engineered biomolecular constructs.

4. Chemical Biology Conjugation Chemistry

Fmoc-D-Asp(All)-OH is applied in chemical biology for preparing aspartate-containing conjugation handles where orthogonal protection supports controlled activation of the side-chain carboxyl group. The allyl ester provides a stable masked acid during peptide coupling and purification steps, while side-chain deprotection reveals a reactive carboxylic acid suitable for coupling to electrophiles such as amines, hydrazides, or linker moieties. The Fmoc group enables clean N-terminal handling during synthesis of labeled peptides, affinity probes, or fragment-based chemical tools, with the D-aspartate stereochemistry supporting specificity in recognition assays. The compound thus serves as a chemically addressable intermediate for generating defined biomolecule conjugates and for constructing reagent sets used in molecular recognition and binding studies.

5. Pharmaceutical Intermediate Preparation

Fmoc-D-Asp(All)-OH is relevant to pharmaceutical intermediate preparation where protected amino acids are manufactured and processed as chiral building blocks for peptide-like active ingredients and process intermediates. The Fmoc-protected amine and allyl-protected side-chain carboxyl group support a protection strategy that reduces side reactions during synthesis scale-up and enables predictable deprotection sequences in downstream manufacturing steps. The D-aspartate stereocenter can be retained through controlled coupling and functional-group transformations, supporting stereochemically consistent intermediate supply for peptide synthesis routes. The compound's functional group pattern supports conversion into activated aspartate derivatives and standardized peptide building blocks, aligning it with fine chemical synthesis and industrial chemical manufacturing practices for chiral intermediate generation.

1. Effect of Short-Term Desiccation, Recovery Time, and CAPA-PVK Neuropeptide on the Immune System of the Burying Beetle Nicrophorus vespilloides

2. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

3. Effect of Probiotic Lactobacillus plantarum on Streptococcus mutans and Candida albicans Clinical Isolates from Children with Early Childhood Caries

4. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

5. GLP-1, exendin-4 and C-peptide regulate pancreatic islet microcirculation, insulin secretion and glucose tolerance in rats