Pharmaceutical Peptides Services
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Peptides are biomolecules made from 20 naturally occurring amino acids linked by covalent bonds, and their unique structure gives them high selectivity and high efficiency. In recent years, with the advancement of bioengineering and chemical synthesis technology, the research and development of pharmaceutical peptides has entered a golden period of development. Up to now, more than 80 pharmaceutical peptides have been approved for marketing worldwide, covering endocrine diseases (such as insulin and GLP-1 analogs), immune disorders (such as cyclosporine) and cardiovascular diseases (such as exenatide).
Fig.1 A key milestone in the field of peptide therapy. (Muttenthaler, Markus, et al., 2021)
What are Pharmaceutical Peptides?
Pharmaceutical peptides are a class of short-chain polymers made up of amino acids linked by peptide bonds, typically consisting of 2 to 50 amino acids. They play an important role in the medical field because they have many unique pharmacological properties, such as high selectivity, high affinity, and low toxicity. Pharmaceutical peptides can be naturally occurring or produced in a laboratory by recombinant DNA technology or chemical synthesis methods.
Pharmaceutical Peptides vs. Research Peptides
There are significant differences between pharmaceutical peptides and research peptides in terms of use, safety, and purpose of use. Pharmaceutical peptides refer to peptide drugs that have passed rigorous research and clinical trials and have been approved by the FDA. These drugs can be used to treat, prevent, or cure specific diseases such as diabetes, cancer, etc. Pharmaceutical peptides are highly selective and specific, allowing them to act directly on specific targets in the body, thereby improving efficacy and reducing side effects. In addition, pharmaceutical peptides usually have a long half-life and are able to maintain a therapeutic effect in vivo for a longer period of time. In contrast, research peptides are primarily used in scientific research and laboratory studies, they are only suitable for in vitro experiments and research work, and are not approved by the FDA for the treatment, prevention, or cure of any disease. Research peptides are typically available in powder form and are used to explore new drug candidates or to validate the mechanism of action of an existing drug. In addition, because the study peptides have not been approved in human clinical trials and the FDA, their safety and efficacy cannot be guaranteed and are not recommended for human treatment.
According to market statistics, pharmaceutical peptides are growing at an annual rate of more than 10%, and their market size is expected to reach tens of billions of dollars by 2030. At the same time, the demand for research peptides, as an important tool for new drug research and development, continues to rise. For example, research-based peptides have significantly shortened the drug discovery cycle and improved screening efficiency in target validation. Pharmaceutical peptides not only have the advantage of reducing side effects, but also overcome the shortcomings of poor stability of traditional drugs through molecular modification. Therefore, peptides have become a hot spot in the pharmaceutical industry.
Table.1 Peptides in Diabetes at Creative Peptides.
Table.2 Peptides in Cancer Research at Creative Peptides.
R&D Process of Pharmaceutical Peptides
The main challenges in the development of pharmaceutical peptides include synthesis, purification and quality control, stability, delivery methods, and high cost. Peptides are composed of a large number of amino acids and have complex spatial structures, which are especially difficult to synthesize medium- and long-term peptides and molecules with complex structures. The purification process is complex and expensive, requiring multiple adjustments to ensure quality control. However, pharmaceutical peptides are easy to be enzymatically hydrolyzed in vivo and have a short half-life, so their stability needs to be improved by various modification technologies. In addition, it is often administered by injection, and patient acceptance is low, limiting its widespread use. R&D and production costs are relatively high, especially in large-scale production, which is difficult to control. According to the report of the Prospective Industry Research Institute, the R&D cost of a new drug in the world has exceeded 1 billion US dollars, with a cycle of more than 10 years, and a large amount of financial support is required, including R&D personnel salary, materials, technology development, equipment purchase and payment of outsourced R&D expenses. As a result, new entrants often face long start-up times and significant financial pressures.
Fig.2 A modular view of the pharmaceutical peptide development cycle. (Lee, Andy Chi-Lung, et al., 2019)
Discovery of Lead Compounds
The discovery of peptide lead compound targets typically involves identifying a protein, or receptor, that is associated with a disease and validating its role in pathophysiology. For example, through genomics and proteomics studies, researchers can identify specific proteins or receptors as potential targets. Integrated genomics uses bioinformatics to analyze the genomic and transcriptome data of toxic animals to identify a large number of venom peptide sequences that can be synthesized or recombined for therapeutic target screening. In addition, phage display technology is also a commonly used screening method, by constructing a large number of peptide libraries, after multiple rounds of screening, to produce high-affinity target conjugates. Peptide lead compounds are screened using a variety of methods, including:
Phage display technology: By constructing a phage display peptide library, peptide sequences with high affinity for the target are screened.
High-throughput screening: High-throughput screening is performed using DNA-encoded compound libraries, RNA display, and other technologies to quickly identify bioactive peptides.
Screening methods based on target proteins: Quantitative determination of biochemical level interactions is performed after mixing candidate peptides with target proteins, and commonly used methods include enzyme-linked immunoassay, fluorescence thermogenesis, nuclear magnetic resonance, etc.
Cell surface display technology: Peptides targeting specific tumor cell surface markers are screened through cell surface display technology to improve treatment efficacy.
Computer-aided design (CAD): Based on the structural information of the target, design peptide sequences that can bind specifically to the target, and use CAD software to predict the spatial structure and affinity of the peptide.
These methods have their own advantages, which can effectively improve the screening efficiency and provide strong support for the research and development of pharmaceutical peptides.
What is peptide drug?
Peptide drug refers to a peptide having a specific therapeutic effect extracted by chemical synthesis, genetic recombination or animal or...
Peptide lead optimization is to improve upon a lead molecule that demonstrates activity at a target of interest by optimizing its potency or selectivity at the target and its absorption...
Pharmaceutical Peptides Design and Optimization
The discovery of pharmaceutical peptide targets often relies on in-depth research into specific biological processes or diseases. For example, G protein-coupled receptors (GPCRs) are one of the largest protein families in the human body, involved in the regulation of a variety of physiological processes, and have been associated with a variety of diseases. At present, more than 475 GPCR drugs have been approved for marketing, of which nearly 50 are pharmaceutical peptides targeting GPCRs. Another example is somatostatin receptor (SSTR2), Tye1002 is a peptide-drug conjugate targeting SSTR2 that has shown promising anti-tumor effects in a variety of tumor cells.
There are several methods for purifying peptides, including organic solvent precipitation, ion exchange chromatography, gel filtration chromatography, affinity chromatography, and high-performance liquid chromatography (HPLC). The organic solvent precipitation method precipitates the peptides by forming a complex between the organic solvent and the peptide in the aqueous phase. Ion-exchange chromatography takes advantage of the charged nature of peptides to achieve separation by means of ion exchange resins. Gel filtration chromatography separates peptide molecules of different sizes by gel pore size, while affinity chromatography uses peptide interactions with specific ligands to achieve highly selective separations. High performance liquid chromatography combines stationary phases and different solvent systems to provide high-resolution and sensitive peptide separations.
Fig.3 Strategies for improving physicochemical properties of peptides. (Lee, Michelle Felicia, and Chit Laa Poh., 2023)
When it comes to peptide modification, common methods include cyclization, glycosylation, phosphorylation, N-methylation, and polyethylene glycol (PEG) modification. Cyclization enhances rigidity and stability by forming disulfide bonds, amide structures, or biphenyl ethers to synthesize cyclic peptides. Glycosylation introduces glycosylated residues into peptides for the treatment of drug-resistant bacterial infections. Phosphorylation is reversible phosphorylation at specific residues to control cellular processes. N-methylation makes peptides more resistant to biodegradation by introducing N-methylated amino acid derivatives, while PEG modification improves hydrolytic stability and biodistribution, extending the half-life of the drug.
There are also various methods of peptide conjugation, with sulfhydryl modifications using either carbodiimide or glutaraldehyde to conjugate the peptide to a carrier protein. Lysine-tyrosine coupling allows the drug to be attached to a side chain group, and artificial amino acid modification achieves coupling by introducing a specific side chain group. In addition, fluorescent labels are used to detect protein activity to aid in drug screening and development, while biotin labels are used in areas such as immunoassays, histochemistry, and flow cytometry.
These methods improve the efficacy and stability of pharmaceutical peptides through different chemical reactions and modifications, and show a wide range of application prospects in clinical applications.
Interested in the use of biologically active proteins and peptides as potential therapeutic agents has grown dramatically in recent years. Although many meaningful studies can be performed...
Leveraging our expertise and knowledge in peptides manufacturing, Creative Peptides provides convenient multiple types of peptide conjugation services to meet the needs of…
Creative Peptides offers hundreds of peptide modifications to meet any research need. These modifications can improve the overall stability of peptide, change the structure to better…
The synthesis methods of peptides are mainly divided into two categories: chemical synthesis and biosynthesis. Among the chemical synthesis methods, solid-phase synthesis is currently the most commonly used method. The peptide chain is constructed by immobilizing the first amino acid on an insoluble resin and then progressively adding other amino acids. This method is suitable for the synthesis of peptide chains with long length and high purity, among which the Fmoc method is favored due to its mild reaction conditions, fewer by-products, and high yields. The liquid-phase synthesis method is mostly used for the synthesis of shorter peptides, and has two strategies: stepwise synthesis and fragment combination, which is suitable for the rapid synthesis of bioactive peptide fragments and peptides containing more amino acids.
Compared with chemical synthesis, biosynthesis uses genetic recombination, fermentation and enzymatic hydrolysis to synthesize the required peptides through biological metabolism. The gene recombination method is suitable for the synthesis of longer peptide chains due to its advantages of strong directionality, high safety and low cost by inserting the gene encoding peptide into the host cell for expression, but it has the disadvantages of long development cycle, difficult isolation and low yield. The fermentation method is to produce natural peptides through the metabolism of microorganisms, although the cost is low, but the application range is limited. Enzymatic hydrolysis uses enzyme-catalyzed ligation of amino acids into peptide chains, which has the advantage of controlling the structure and purity of peptides, but the reaction conditions are complex and require specific enzymes and substrates. Selecting the appropriate synthesis method requires a comprehensive consideration of the length, structural complexity, and application field of the target peptide.
The recognition by Hofmeister and Emil Fischer that the structure of proteins is best represented by chains of amino-acids linked to each other through amide bond was preceded by...
There are a variety of peptide analysis methods, including mass spectrometry, high-performance liquid chromatography, nuclear magnetic resonance (NMR) and amino acid analysis, all of which have their own unique characteristics and applications. Mass spectrometry is one of the most commonly used and important methods, as it is possible to determine the molecular weight and sequence of peptides by measuring the mass/charge ratio of peptide ions, and is also used for quantitative analysis. Mass spectrometry is of great significance in pharmaceutical peptides development, disease diagnosis and treatment, and can provide key support for the quality evaluation of pharmaceutical peptides. HPLC is commonly used for the purity analysis and content determination of peptides, which is suitable for accurate quantification, but the operation is complex and requires specialized instruments and techniques. Nuclear magnetic resonance is increasingly used as a means of analysis, especially for small molecule peptides, which can provide high-resolution structural information to help resolve the secondary structure and spatial conformation of peptides. Amino acid analysis is a quantitative analysis of amino acids by acid hydrolysis of peptides, which has high accuracy, but also has certain limitations.
Peptide analysis is important for drug development, biological activity research, and disease diagnosis and treatment. Through analytical techniques, researchers can optimize the design and synthesis of pharmaceutical peptides, improve their pharmacokinetic properties and stability, and ensure the quality, safety, and efficacy of the drugs. In addition, peptide analysis can help to deeply understand the relationship between peptide structure and function, and promote the development of new drugs. Especially in disease diagnosis, mass spectrometry can be used to quantitatively analyze disease-related peptides, which is helpful for the early diagnosis and treatment of diseases. In biologics quality control, analytical techniques are used to assess the quality and purity of biologics to ensure they meet regulatory requirements. As technology advances, these analytical methods will become more precise and efficient, providing long-term support for biomedical research, drug development, and disease treatment.
The recognition by Hofmeister and Emil Fischer that the structure of proteins is best represented by chains of amino-acids linked to each other through amide bond was preceded by...
Overview of drug formulation
Pharmaceutical products are formulated products with specific dosage forms for efficient delivery and product stability. Formulation development...
At Creative Peptides, we are dedicated to advancing this innovative therapy through our comprehensive neoantigen peptides vaccines services. By leveraging...
Our Advantages
Our services are based on an advanced technology platform to provide efficient and customized services. Here are the key technical highlights:
Precision synthesis technology: Peptide solid-phase synthesis (SPPS) and liquid phase synthesis (LPPS) technologies ensure high purity and high efficiency. Our capabilities extend to delivering pharmaceutical-grade peptides that fully comply with GMP standards, meeting the rigorous requirements of drug development and production.
Diversified modification capabilities: Covering cyclization, PEG, introduction of unnatural amino acids and other modifications.
High-throughput screening platform: Rapid screening of powerful peptide leads.
Strict quality management: The whole process of quality control from R&D level to GMP level.
With the increasing demand for medicine, the market size of pharmaceutical peptides continues to expand. Creative Peptides is committed to providing full-process solutions to provide stronger technical support for drug development. A new era of pharmaceutical peptides has arrived, and we look forward to working with researchers and companies around the world to welcome more innovations.
References
- Muttenthaler, Markus, et al., Trends in peptide drug discovery. Nature reviews Drug discovery 20.4 (2021): 309-325.
- Lee, Andy Chi-Lung, et al., A comprehensive review on current advances in peptide drug development and design. International journal of molecular sciences 20.10 (2019): 2383.
- Lee, Michelle Felicia, and Chit Laa Poh. Strategies to improve the physicochemical properties of peptide-based drugs. Pharmaceutical Research 40.3 (2023): 617-632.
