Product Name: Fmoc-Cys-Asp10
Sequence: {Fmoc}-CDDDDDDDDDD
Purity: 95%
Storage : Sealed storage, away from moisture and light
CAS.NO.: 2407782-70-9
CHEMICAl FORMULA: C58H67N11O34S
Molar Mass: 1494.27
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
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
INCHIKEY: CNKQRGXYKSQSRU-SJPCSGTBSA-N
INCHI: InChI=1S/C58H67N11O34S/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/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)/t26-,27-,28-,29-,30-,31-,32-,33-,34-,35-,36-/m0/s1
Application: Fmoc-Cys-Asp10 is a non-releasable oligopeptide linker used in the synthesis and design of releasable oligopeptide linker systems. It contains a cysteine residue suitable for conjugation and a poly-aspartic acid segment that can support hydrophilic linker construction and bone-targeting conjugate research. Releasable oligopeptide linkers are useful for delivering therapeutic or imaging agents to bone fracture-homing peptides, enabling targeted localization at injured bone sites. Fmoc-Cys-Asp10 is widely applied in peptide synthesis, drug delivery research, bone-targeted biomolecule design, and regenerative medicine studies focused on fracture repair and improved femur healing outcomes.
Current Research: Overview Fmoc-Cys-Asp10 is a synthetic oligopeptide linker composed of an Fmoc-protected cysteine residue followed by a chain of ten aspartic acid residues. It may be represented as Fmoc-Cys-(Asp)10 or Fmoc-CDDDDDDDDDD. This compound is described as a non-releasable oligopeptide linker and is involved in the synthesis of releasable oligopeptide linker systems. In current peptide chemistry and drug delivery research, Fmoc-Cys-Asp10 is especially relevant to bone-targeted delivery, fracture-homing peptide conjugates, and localized therapeutic agent release. Releasable oligopeptide linkers have been studied for delivering bioactive agents to bone fracture-homing oligopeptides, with research showing reduced healing time in fractured femur models. In this context, Fmoc-Cys-Asp10 is best understood as a linker-related peptide building block used in the design of more complex conjugates for bone repair research. Unlike conventional drug molecules, Fmoc-Cys-Asp10 is not primarily studied for direct pharmacological activity. Its importance lies in its structural features: an Fmoc-protected amino group, a cysteine residue suitable for conjugation chemistry, and a highly acidic Asp10 sequence that may support interaction with mineralized bone surfaces. These characteristics make it valuable in research involving oligopeptide linker synthesis, bone fracture-targeted delivery, and peptide-drug conjugate design. Structural Characteristics of Fmoc-Cys-Asp10 Fmoc-Cys-Asp10 contains three major functional components: the Fmoc protecting group, cysteine, and a deca-aspartic acid chain. The Fmoc group is widely used in peptide synthesis to protect the N-terminal amino group during stepwise assembly. In solid-phase peptide synthesis, Fmoc chemistry enables controlled peptide elongation and selective deprotection. For a linker such as Fmoc-Cys-Asp10, the Fmoc group helps maintain synthetic control and can support downstream modification or incorporation into larger molecular systems. The cysteine residue introduces a chemically reactive thiol side chain. Cysteine is frequently used in bioconjugation because its sulfhydryl group can react with maleimide groups, disulfide-forming reagents, haloacetamides, and other thiol-reactive chemistries. This makes Fmoc-Cys-Asp10 useful for attaching peptide chains to therapeutic agents, carriers, targeting groups, or other linker components. The Asp10 segment contains ten consecutive aspartic acid residues. This gives the molecule a strongly acidic and anionic character. Aspartic acid-rich sequences are of interest in bone-targeting research because acidic peptides can interact with calcium-rich mineral surfaces, including hydroxyapatite-like structures found in bone. This feature is particularly relevant for fracture-targeted delivery, where exposed or actively remodeling mineral surfaces may provide binding opportunities for acidic oligopeptides. Role as a Non-Releasable Oligopeptide Linker Fmoc-Cys-Asp10 is described as a non-releasable oligopeptide linker. In linker design, “non-releasable” generally refers to a linker that remains attached to the carrier or conjugate after delivery or processing. This differs from a releasable linker, which is designed to break under specific biological or chemical conditions. However, Fmoc-Cys-Asp10 is also involved in the synthesis of releasable oligopeptide linker systems. This means it can function as a structural or synthetic component in larger linker designs where another bond or segment provides controlled release. In such systems, the Asp10 sequence may contribute to bone localization, while the releasable portion of the conjugate allows the therapeutic agent to be liberated at or near the fracture site. This distinction is important for accurate product communication. Fmoc-Cys-Asp10 itself should not be described as the complete releasable delivery system. Rather, it is a non-releasable oligopeptide linker or linker intermediate that can participate in the preparation of releasable oligopeptide conjugates. Relevance to Bone Fracture-Homing Oligopeptide Research Bone fracture repair involves multiple biological stages, including inflammation, callus formation, angiogenesis, mineralization, and remodeling. Although many fractures heal naturally, delayed healing and nonunion remain significant clinical challenges. Targeted drug delivery is being investigated as a strategy to concentrate therapeutic agents at fracture sites while minimizing systemic exposure. Releasable oligopeptide linker systems have been used to deliver agents to bone fracture-homing oligopeptides. These systems are designed to guide a bioactive molecule to the fracture region and release it locally. Research has reported that such strategies can reduce healing time in fractured femur models, suggesting that site-specific delivery may improve the efficiency of bone repair. Fmoc-Cys-Asp10 is relevant to this research direction because of its acidic Asp10 sequence and cysteine-based conjugation potential. The Asp-rich chain may support bone mineral affinity, while the cysteine residue can provide a handle for chemical attachment. Together, these features make Fmoc-Cys-Asp10 useful in the construction of peptide-based delivery systems for skeletal repair studies. Aspartic Acid-Rich Peptides and Bone Targeting Aspartic acid-rich peptides are frequently studied in bone-targeted delivery because of their ability to associate with mineralized tissue. Bone contains calcium phosphate mineral, and acidic residues such as aspartic acid can interact with calcium ions and hydroxyapatite-like surfaces. The repeated aspartic acid sequence in Fmoc-Cys-Asp10 gives it a high density of carboxyl groups, which may enhance interaction with bone mineral. This mineral-affinity mechanism is different from receptor-mediated targeting. Instead of binding to a specific protein receptor, acidic oligopeptides rely on physicochemical interactions with mineralized matrices. This can be useful in fracture research because injured bone exposes new mineral surfaces and undergoes active remodeling. The Asp10 motif may therefore support localization of conjugates near bone injury sites. In research design, this type of targeting can be used to deliver small molecules, peptides, imaging agents, or regenerative compounds to skeletal tissue. Fmoc-Cys-Asp10 provides a convenient peptide framework for exploring these possibilities. Releasable Linker Systems for Localized Agent Delivery A major goal of fracture-targeted delivery research is to transport active agents to the damaged bone region and release them in a controlled manner. Releasable oligopeptide linkers are designed for this purpose. They can connect a therapeutic agent to a targeting peptide and then release the agent under defined conditions. These release mechanisms may involve enzymatic cleavage, hydrolysis, pH-sensitive bonds, redox-sensitive bonds, or other biologically responsive chemistries. In a fracture-homing conjugate, the targeting segment directs the molecule toward the injury site, while the linker controls payload retention and release. Fmoc-Cys-Asp10 can contribute to the assembly of such systems. Its cysteine residue may be used for conjugation, while the Asp10 sequence can provide bone-targeting character. When combined with a releasable chemical bond or peptide sequence, it can help form conjugates designed for localized drug delivery in bone repair models. Application in Fracture Healing Research Releasable oligopeptide linker systems have been studied for delivering agents that influence bone healing. One research direction involves delivering bioactive compounds to a bone fracture-homing oligopeptide to accelerate fracture repair. In this type of platform, the therapeutic agent is not administered as a freely circulating drug. Instead, it is attached to a targeting structure that can accumulate near the fracture site. This approach may offer several advantages. Localized delivery may increase the concentration of the active agent at the damaged bone region. It may reduce off-target exposure in healthy tissues. It may also allow lower effective doses by improving distribution to the intended site. Fmoc-Cys-Asp10 is useful in this context because it supports the design of peptide-based linkers with bone-affinity properties. While the final biological effect depends on the complete conjugate, including the payload, targeting sequence, release mechanism, and dosing strategy, Fmoc-Cys-Asp10 provides an important chemical component for linker development. Potential Research Applications Fmoc-Cys-Asp10 may be used in several research fields related to peptide chemistry and bone-targeted delivery. In bone fracture-targeted drug delivery, it may help researchers design conjugates that localize therapeutic agents near damaged skeletal tissue. In releasable oligopeptide linker synthesis, it may serve as a building block or intermediate for constructing linker systems that combine targeting and controlled release. In peptide-drug conjugate research, Fmoc-Cys-Asp10 can provide both a conjugation handle and an acidic peptide sequence, making it useful for attaching bioactive molecules to bone-targeting structures. In biomaterials research, Asp-rich peptides may be studied for interactions with hydroxyapatite, calcium phosphate materials, mineralized scaffolds, or bone-mimetic surfaces. In orthopedic regenerative medicine, linker systems derived from Fmoc-Cys-Asp10 may support studies focused on accelerating fracture repair, improving localized delivery, and reducing systemic exposure of regenerative agents. Research Considerations Researchers using Fmoc-Cys-Asp10 should consider several important factors. First, the compound should be handled as a linker or linker intermediate rather than as a complete therapeutic construct. Its biological relevance depends on how it is incorporated into a larger conjugate. Second, the Asp10 sequence introduces strong acidity and multiple carboxyl groups. This can affect solubility, purification, counterion behavior, and conjugation conditions. Buffer pH, ionic strength, and metal ion content may influence its behavior during experiments. Third, cysteine reactivity must be controlled carefully. The thiol group can undergo oxidation or side reactions if not properly protected or handled. Reducing conditions, oxygen exposure, and storage conditions may affect conjugation efficiency. Fourth, release behavior must be experimentally validated. Since Fmoc-Cys-Asp10 is described as non-releasable, any controlled release function depends on the complete linker system and the specific release-sensitive bond or sequence used. Analytical methods such as HPLC, LC-MS, MALDI-TOF MS, peptide mapping, stability testing, binding assays, and release assays may be used to evaluate purity, identity, conjugation efficiency, mineral affinity, and payload release. Future Research Directions Fmoc-Cys-Asp10 reflects a broader trend in drug delivery research: the development of targeted molecular systems that localize therapeutic activity at specific tissue sites. In skeletal repair, this approach is particularly attractive because fracture healing requires coordinated biological signaling at a defined anatomical location. Future studies may explore optimized Asp-rich sequences, improved releasable linker chemistries, new payloads for bone repair, and conjugates with enhanced fracture-site selectivity. Researchers may also investigate how oligopeptide length, charge density, cysteine-based conjugation chemistry, and release kinetics affect bone localization and healing outcomes. Fmoc-Cys-Asp10 may continue to be useful as a synthetic linker component for these investigations. Its combination of Fmoc protection, cysteine reactivity, and Asp10 mineral-affinity potential makes it a valuable tool for designing bone-targeted peptide conjugates. Conclusion Fmoc-Cys-Asp10 is a specialized non-releasable oligopeptide linker involved in the synthesis of releasable oligopeptide linker systems. Structurally, it contains an Fmoc-protected cysteine and ten aspartic acid residues, giving it both conjugation utility and acidic peptide character. Current research connects releasable oligopeptide linkers with the delivery of agents to bone fracture-homing oligopeptides, a strategy that has been studied for reducing fractured femur healing times. Fmoc-Cys-Asp10 is therefore relevant to bone-targeted drug delivery, peptide-drug conjugate design, fracture repair research, and oligoaspartate-based skeletal targeting. As targeted regenerative medicine continues to develop, Fmoc-Cys-Asp10 may serve as a useful peptide linker building block for constructing localized delivery systems designed to improve fracture healing and bone repair research outcomes.
Get a Quote
LinkPeptide
