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High-quality peptides at competitive prices are just one click away! Starting at €1.66 per amino acid, you can generate synthetic peptides up to 150 residues with an unlimited range of modifications and pay only if you’re satisfied with your order. In just a few clicks, fill out the form to receive an instant quote and order directly from our shop using the secure online payment system. Start your custom peptide synthesis now!
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Peptide synthesis up to 150 AA
ProteoGenix can synthesize peptides up to 150 AA.
Unlimited range of modifications
ProteoGenix offers an unlimited range of peptide modifications.
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Your project is our priority so we will start from the beginning until we get the right peptide or you won’t pay a thing.
At ProteoGenix, we offer recombinant expression and semisynthesis
(ligation of synthetic and recombinant fragments) in addition to the
standard Fmoc solid-phase synthesis. If you are working with complex
structures, reach out to our team to learn how we can help.
DISCOVER OUR SOLUTIONS
If you are looking for an expert’s advice to help you maximize the stability and yield of your synthetic peptide while keeping production costs low, reach out to our team for more information.
The most commonly used method to test solubility is based on charge determination. For small peptides with up to 5 amino-acids, distilled water remains the first option. For other cases, you can refer to this guide:
Synthetic antigenic peptides represent powerful tools for polyclonal or monoclonal antibody generation and as components of peptide vaccines. For these applications, peptides need to be designed with two properties in mind: antigenicity and immunogenicity.The first term is used to describe the ability of an antigen to interact with an antibody’s functional binding site, while the second term describes a peptide’s ability to elicit a humoral an/or cellular immune response. For effective vaccine and antibody production, peptides must have both properties.
Enhancing peptide antigenicity can be achieved by:
Peptide immunogenicity can be maximized by coupling synthetic peptides with carriers keeping the following recommendations in mind:
Many peptide drugs are generated by chemical modification of natural molecules. These drugs remain invaluable for the treatment of multiple metabolic diseases.
Vaccines are considered one of the most successful strategies of modern medicine. Conventional vaccines have relied heavily in inactive pathogens to elicit an immune response, making them hard to produce. In contrast, peptide vaccines are increasingly considered as a cost-effective, safer, and highly specific alternative.
Peptides for tissue engineering
The discovery of cell adhesion and self-assembling peptides has opened up a new window of opportunity in tissue engineering applications. These peptides are increasingly used as bioactive molecules to support cellular growth and tissue regeneration.
Drug & Gene Delivery
Cell-penetrating peptides and self-assembling peptides are two increasingly important bioactive components of advanced gene and drug delivery applications . In comparison to conventional methods that make use of viral vectors, peptides are much easier to synthesize, thus, helping make the technology more accessible and widespread.
Many personal care products harness the beneficial properties of cosmetic peptides . Small peptides able to cross the skin barrier are often incorporated in cosmetics due to their easy diffusion allied to their protective and regenerative properties. Peptides with antimicrobial properties are also often incorporated in creams to prevent and treat several well-known skin conditions.
Solid-phase peptide synthesis has dominated the market for custom production in the last couple of decades. The method, initially developed in the 1950s, has matured into a technology that remains unparalleled in terms of automation, cost-effectiveness, scalability, lead times, and yields.
This method is traditionally carried out on a solid support in a stepwise manner from the C to the N terminus. Nα-protected amino acids are used to control the direction of the synthesis process and thus minimize side reactions. Today, solid-phase synthesis makes use of two major N-terminus protective groups: Boc (t-butyloxycarbonyl) and Fmoc (9-fluorenylmethoxycarbonyl).
In addition to these protective groups, permanent protection groups are often attached to side chains. These groups prevent unwanted branching and can withstand several cycles of chemical treatment during the synthesis process. They are only removed in the final stage of the process using strong acids. Benzyl (Bzl) and tert-butyl (tBu) are two of the most widely used side chain protection groups.
The stepwise synthesis of peptides is carried out as follows:
The use of strong chemicals to produce synthetic peptides may offer a challenge when it comes to purification. To overcome this limitation, liquid-phase synthesis is often employed to achieve GMP-grade peptide production. Despite being significantly more time-consuming and leading to lower yields than solid-phase synthesis, liquid-phase methods are still sparingly used to produce highly pure short peptides (<10 AA) for some applications.
Both solid-phase and liquid-phase synthesis are chemical methods for linear peptide production. When large peptides with complex secondary or tertiary structures are required, recombinant expression is a much better alternative. However, despite being able a good method to produce long peptides, recombinant expression suffers from an important disadvantage – it is restricted to natural amino acids produced and processed by the host organism.
For this reason, when peptides with complex structures and unnatural amino acids need to be produced, a semisynthetic approach may be ideal.
Despite the high efficiency of most peptide synthesis methods, many of these processes may still generate undesired impurities due to incomplete deprotection, unwanted reactions between free protecting groups, truncation and/or deletion of amino acids, isomers, and other side products.
Removal of these impurities is recurrently achieved by using one or several purification techniques:
Among these, RP-HPLC is the most widely used process of purification. Unlike conventional HPLC that separates products according to the concentration of polar solvents on the mobile phase, RP-HPLC captures hydrophobic molecules from aqueous solutions and releases them in function of their hydrophobicity. This makes it easier to separate correctly synthesized peptides from undesired impurities.
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