Product Name: Fmoc-Cys-Asp10 TFA
Sequence: {Fmoc}-CDDDDDDDDDD
CHEMICAl FORMULA: C60H68F3N11O36S
Molarmass: 1608.29
Purity: 95%
Form: White to off-white Solid
Storage : Sealed storage, away from moisture
SMILES: C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)N[C@@H](CS)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O.C(=O)(C(F)(F)F)O
IUPACNAME: (2S)-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2S)-3-carboxy-2-[[(2R)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-sulfanylpropanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]butanedioic acid;2,2,2-trifluoroacetic acid
INCHIKEY: BIFUHFPXQBJYJF-KDYAZIBBSA-N
INCHI: InChI=1S/C58H67N11O34S.C2HF3O2/c70-37(71)9-26(47(90)60-28(11-39(74)75)49(92)62-30(13-41(78)79)51(94)64-32(15-43(82)83)53(96)66-34(17-45(86)87)55(98)68-35(57(100)101)18-46(88)89)59-48(91)27(10-38(72)73)61-50(93)29(12-40(76)77)63-52(95)31(14-42(80)81)65-54(97)33(16-44(84)85)67-56(99)36(20-104)69-58(102)103-19-25-23-7-3-1-5-21(23)22-6-2-4-8-24(22)25;3-2(4,5)1(6)7/h1-8,25-36,104H,9-20H2,(H,59,91)(H,60,90)(H,61,93)(H,62,92)(H,63,95)(H,64,94)(H,65,97)(H,66,96)(H,67,99)(H,68,98)(H,69,102)(H,70,71)(H,72,73)(H,74,75)(H,76,77)(H,78,79)(H,80,81)(H,82,83)(H,84,85)(H,86,87)(H,88,89)(H,100,101);(H,6,7)/t26-,27-,28-,29-,30-,31-,32-,33-,34-,35-,36-;/m0./s1
Application: Fmoc-Cys-Asp10 (TFA) is a non-releasable oligopeptide linker used in the development and synthesis of releasable oligopeptide linker systems. Its cysteine residue provides a functional handle for conjugation, while the poly-aspartic acid segment contributes hydrophilicity and bone-targeting linker design potential. Releasable oligopeptide linkers are valuable for delivering therapeutic or imaging agents to bone fracture-homing oligopeptides, supporting targeted localization at fracture sites. Fmoc-Cys-Asp10 (TFA) is widely used in peptide synthesis, drug delivery research, bone-targeting conjugate development, and regenerative medicine studies focused on improving fracture repair and reducing femur healing time.
Current Research: Overview Fmoc-Cys-Asp10 (TFA) is a synthetic oligopeptide linker with the shortened sequence Fmoc-CDDDDDDDDDD, consisting of an Fmoc-protected cysteine followed by ten aspartic acid residues. It is supplied as the trifluoroacetate salt and is described as a non-releasable oligopeptide linker involved in the synthesis of releasable oligopeptide linkers. Product references report its molecular formula as C60H68F3N11O36S and molecular weight as 1608.29. In current biomaterials and drug delivery research, Fmoc-Cys-Asp10 (TFA) is especially relevant to bone-targeted delivery systems. Oligoaspartic acid sequences have strong interest in skeletal targeting because acidic amino acid-rich peptides can interact with mineralized bone surfaces. In fracture-healing research, releasable oligopeptide linker systems have been used to deliver therapeutic agents to bone fracture-homing oligopeptides, with reported reductions in fractured femur healing time in mouse models. For SEO product-page use, Fmoc-Cys-Asp10 (TFA) can be positioned as a specialized peptide linker for bone-targeted conjugate design, fracture-localized drug delivery, and oligopeptide linker synthesis. It is not a conventional small-molecule drug or a general ADC linker. Instead, its value lies in its peptide architecture, acidic Asp10 domain, Fmoc-protected cysteine residue, and utility in constructing more complex releasable linker systems. Structural Features of Fmoc-Cys-Asp10 (TFA) The structure of Fmoc-Cys-Asp10 (TFA) combines three important design elements: an Fmoc protecting group, a cysteine residue, and a deca-aspartic acid chain. The Fmoc group is widely used in solid-phase peptide synthesis as an N-terminal protecting group. In linker research, Fmoc protection can help control stepwise synthesis and allow the peptide intermediate to be incorporated into more complex conjugation workflows. The cysteine residue provides a chemically useful thiol-containing amino acid. Cysteine is frequently used in conjugation chemistry because its sulfhydryl group can participate in reactions with maleimide, disulfide, or other thiol-reactive groups. In linker design, cysteine can provide a site for attaching a payload, carrier, spacer, or release-sensitive component. The Asp10 sequence, composed of ten aspartic acid residues, gives the molecule a highly acidic, anionic character. This oligoaspartate region is central to its relevance in bone-targeting research. Acidic oligopeptides can show affinity for mineral-rich bone surfaces, particularly areas of active bone remodeling or exposed hydroxyapatite. This feature makes Asp-rich sequences attractive for targeted skeletal delivery strategies. Role in Releasable Oligopeptide Linker Synthesis Fmoc-Cys-Asp10 (TFA) is described as a non-releasable oligopeptide linker that is involved in the synthesis or preparation of releasable oligopeptide linkers. This distinction is important for accurate product copy. A non-releasable linker remains attached to the conjugated structure after delivery or processing, whereas a releasable linker is designed to separate under defined biological or chemical conditions. Releasable linkers may respond to enzymes, pH, redox conditions, hydrolysis, or other microenvironmental triggers. In the context of fracture-targeted therapy, a releasable linker can help carry an active agent to a bone injury site and then enable local release of the therapeutic payload. Fmoc-Cys-Asp10 (TFA) may therefore be used as an intermediate or building block in the preparation of more advanced linker-drug or linker-peptide conjugates. Its cysteine residue can support conjugation, while its Asp10 sequence can contribute to fracture-site homing or bone mineral affinity. This makes it useful in research workflows where the goal is to connect a therapeutic agent to a bone-targeting oligopeptide through a designed linker system. Bone Fracture-Homing Oligopeptide Research Bone fracture repair is a complex biological process involving inflammation, angiogenesis, cartilage formation, bone formation, and remodeling. Although many fractures heal naturally, delayed union and nonunion remain major challenges in orthopedics. Targeted delivery strategies are being explored to concentrate regenerative agents at fracture sites while reducing unwanted systemic exposure. A key study reported that conjugating dasatinib to a bone fracture-homing oligopeptide through a releasable linker reduced fractured femur healing times in mice by about 60%, without overt off-target toxicity or remodeling of nontraumatized bone. In the reported model, healthy bone density, normal bone volume, and healthy mechanical properties at the fracture site were achieved after about 3–4 weeks in dasatinib-targeted mice, compared with about 8 weeks in PBS-treated controls. This research provides the biological context for Fmoc-Cys-Asp10 (TFA). The compound itself should be described as a linker or linker intermediate, not as the therapeutic agent. However, it is relevant to the design of linker systems that deliver agents to fracture-homing oligopeptides. Its Asp-rich structure may support targeted interaction with bone fracture surfaces, while its cysteine-containing design enables conjugation chemistry. Importance of Aspartic Acid-Rich Peptides in Bone Targeting Oligoaspartic acid peptides are important in bone-targeted delivery because of their affinity for mineralized tissue. Bone mineral contains hydroxyapatite-like calcium phosphate structures. Acidic peptides, especially those rich in aspartic acid or glutamic acid, can interact with calcium-rich mineral surfaces through electrostatic and coordination interactions. The Asp10 domain in Fmoc-Cys-Asp10 (TFA) gives the molecule a strong acidic profile. This feature may be useful in the design of conjugates intended to localize near sites of bone turnover, fracture repair, or mineral exposure. In fracture sites, active remodeling and newly exposed mineral surfaces may provide opportunities for targeted accumulation of acidic oligopeptide-based conjugates. This strategy differs from antibody-based targeting or receptor-ligand targeting. Instead of relying on a cell-surface antigen, acidic oligopeptide targeting is based on the physicochemical interaction between the peptide and bone mineral. This makes Fmoc-Cys-Asp10 (TFA) relevant to biomaterials, orthopedic drug delivery, skeletal regeneration, and fracture-repair research. Releasable Linkers and Localized Drug Release A major challenge in bone repair pharmacology is delivering enough active agent to the fracture site without causing systemic toxicity. Many bioactive agents can influence osteoblasts, osteoclasts, immune cells, or angiogenic pathways, but systemic administration may produce off-target effects. Linker-based delivery systems aim to solve this problem by controlling where and when the active agent is released. In a fracture-homing conjugate, the targeting oligopeptide directs the construct toward the fracture region. The linker then determines whether the payload remains attached or is released locally. A releasable oligopeptide linker can help ensure that the active agent becomes available at the target site, supporting bone repair while limiting broader exposure. Fmoc-Cys-Asp10 (TFA) is relevant because it participates in the synthesis of such releasable oligopeptide linker systems. Its structure can support the assembly of conjugates in which a therapeutic agent, targeting sequence, and release-sensitive linkage are combined into a single delivery construct. Potential Applications in Current Research Fmoc-Cys-Asp10 (TFA) may be used in several research areas related to peptide chemistry and bone-targeted delivery. In bone fracture-targeted drug delivery, it may serve as a linker intermediate for designing conjugates that localize therapeutic agents at fracture sites. In releasable linker synthesis, it can be used as part of workflows to construct oligopeptide-based linker systems with controlled payload release. In oligoaspartate peptide research, it provides an Asp10-containing structure for studying bone mineral affinity, peptide conjugation, and skeletal targeting. In orthopedic regenerative research, linker systems derived from Fmoc-Cys-Asp10 (TFA) may support the development of localized delivery strategies for agents that influence bone formation, remodeling, or repair. In peptide-drug conjugate design, its cysteine residue and acidic peptide chain make it relevant to conjugates requiring both chemical attachment and mineral-targeting behavior. Research Considerations When using Fmoc-Cys-Asp10 (TFA), researchers should consider the distinction between the linker intermediate and the final releasable conjugate. The product itself is described as non-releasable, while the downstream releasable oligopeptide linker system is used for payload delivery. Product copy should avoid implying that Fmoc-Cys-Asp10 (TFA) alone reduces fracture healing time. The reported healing benefit is associated with a complete conjugate system involving a therapeutic agent, a fracture-homing oligopeptide, and a releasable linker. Solubility, charge state, and salt form are also important. The TFA salt form may influence handling, purification, and formulation. The Asp10 sequence introduces multiple carboxylate groups, making pH and counterion conditions important during synthesis and conjugation. Analytical validation is essential for linker-based conjugates. Researchers may use HPLC, LC-MS, MALDI-TOF MS, amino acid analysis, peptide mapping, and stability testing to confirm sequence integrity, purity, conjugation efficiency, and release behavior. Future Research Directions The study of Fmoc-Cys-Asp10 (TFA)-related linker systems reflects a broader trend in targeted regenerative medicine: the movement from systemic drug administration toward site-specific delivery. Bone fracture-homing oligopeptides, acidic peptide sequences, and releasable linkers offer a way to concentrate therapeutic activity at damaged skeletal tissue. Future research may explore new payloads beyond dasatinib, improved release-sensitive linker chemistries, optimized Asp-rich targeting sequences, and combinations with biomaterial scaffolds or injectable delivery systems. Studies may also investigate how peptide length, charge density, linker stability, and release kinetics influence fracture-site accumulation and bone-healing outcomes. As orthopedic drug delivery advances, Fmoc-Cys-Asp10 (TFA) may remain a useful building block for synthesizing bone-targeted peptide conjugates. Its combination of Fmoc protection, cysteine-mediated conjugation potential, and Asp10 mineral-targeting character makes it valuable for research into localized skeletal therapeutics. Conclusion Fmoc-Cys-Asp10 (TFA) is a specialized non-releasable oligopeptide linker used in the synthesis of releasable oligopeptide linker systems. With the shortened sequence Fmoc-CDDDDDDDDDD, it contains an Fmoc-protected cysteine and a deca-aspartic acid chain that is relevant to bone-targeted conjugate design. Current research connects releasable oligopeptide linkers with the delivery of therapeutic agents to bone fracture-homing oligopeptides, a strategy reported to reduce fractured femur healing times in mouse models. Fmoc-Cys-Asp10 (TFA) is therefore useful for studies involving bone fracture-targeted drug delivery, oligoaspartate-based skeletal targeting, and peptide linker synthesis. Its role is best understood as a chemical building block for constructing advanced conjugates designed to improve localized delivery and controlled release in bone repair research.
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