Peptide dimers are a powerful tool in modern biochemistry and pharmacology with enhanced affinity, stability, and immune response. At CD Formulation, our scientists leverage extensive expertise in custom peptide synthesis to utilize advanced chemoselective dimerization methods. Our innovative approach ensures the highest quality and functionality of peptide dimers, tailored to the specific needs of drug development, therapeutic applications, and vaccine design.
Peptide dimers are two peptide molecules that are linked together. In comparison to the monomeric form, peptide dimers usually have more advantages as follows:
Peptide dimers, those intriguing molecular constructs, often parlay a remarkable elevation in stability compared to their solitary monomer counterparts. This heightened resilience springs from a symphony of additional intermolecular interactions weaving through the peptide chains, effectively thwarting the inevitable onslaught of degradation and denaturation.
The effect of dimerization doesn't stop at stability, it also serves to amplify the affinity of peptides for their respective targets, notably including GPCR ligands. This augmentation of binding strength metamorphoses the efficacy of peptides, transforming them into formidable allies in the realms of drug innovation and therapeutic exploration.
In the vaccine field, the conglomeration of peptide multimers—exemplified by constructs like MAPs—unleashes a cascade of robust immune responses. Their multivalent architecture bestows these peptides with an extraordinary ability to capture the attention of the immune system, catalyzing recognition and activation.
Fig. 1 Synthesis of chemically linked peptide dimers. (Schäffer L, et al., 2003)
CD Formulation stands at the forefront of dimer peptide synthesis, delivering exceptional services that resonate across the globe. Our sophisticated synthesis protocols intertwine seamlessly with advanced peptide analytical technologies, enabling us to tackle a spectrum of challenges inherent in the intricate realm of peptide therapeutics development and production.
We provide a wide range of services, including but not limited to:
In CD Formulation's peptide synthesis lab, chemistries used for peptide dimerization often utilize chemoselective reactions between unprotected peptides. These methods include the formation of Cys-maleimide thioethers, disulfide bonds, and triazole formation via click chemistry. In addition to these chemoselective methods, we also use protected peptide fragments to achieve dimerization, particularly when synthesizing dimers linked by amides. This approach allows for greater control over the structure and properties of the dimer.
Method | Features | Structure |
Cycloserine-maleimide thioether bond | High stability and easy to form. | ![]() |
Disulfide bond | Has reversible properties and is often used in biological binding. | ![]() |
Triazole (click chemistry) | High specificity and efficiency. | ![]() |
Amidation | Easy to control the structure and properties of dimers. | ![]() |
The pharmaceutical industry uses peptide dimers to develop new drugs with improved properties. Enhanced binding affinity and stability make peptide dimers attractive candidates for targeting specific receptors and pathways in the body.
Therapeutic peptides benefit from dimerization, with increased efficacy and longer duration of action. This is particularly important for chronic disease treatments, where sustained activity of the peptide is critical for effective management.
In vaccine design, peptide dimers and multimers can significantly enhance immune responses. By presenting multiple copies of an antigen, these peptides can better stimulate the immune system, resulting in more effective vaccines.
In addition to peptide synthesis capabilities, CD Formulation combines flexible GMP manufacturing facilities with cutting-edge peptide analytical knowledge to provide a full range of quality control testing services to accelerate the commercialization of your products, including:
Published Data
Technology: Intermolecular Triazole Bridge Strategy
Journal: Peptides.
IF: 3.713
Published: 2017
Results:
The authors designed and synthesized a series of side-chain hybrid dimer peptides J-AA (Anoplin-Anoplin), J-RR (RW-RW), and J-AR (Anoplin-RW) based on the bee peptide Anoplin and the arginine- and tryptophan-rich hexapeptide RW through click chemistry and evaluated their antibacterial activity. The results showed that all dimer analogs had 4-16 times higher antibacterial activity against bacterial strains than the parent peptides, and these dimer analogs could rapidly kill bacteria at 1 and 2×MIC and significantly reduce the initial inoculum within the first 2-6 hours. The in vivo antibacterial activity was evaluated in a mouse model infected with Escherichia coli. The results showed that when injected intraperitoneally once at a dose of 5 mg/kg, the bacterial load of all mixed dimer analogs was significantly lower than that of the untreated control group, among which J-RR could effectively treat mice infected with methicillin-resistant (MRSA) strains.
Fig. 2 The time-killing kinetics of three hybrid peptides against multidrug-resistant S.aureus 725. (Liu B, et al., 2017)
CD Formulation has extensive experience with peptide dimer design and synthesis. Please don't hesitate to contact us if you are interested in our services. We look forward to cooperating with you.
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