Empowering Peptide Innovation - Founded in 2001, Iris Biotech provides scientists in both industry and academia with innovative and rare compounds, while also being your reliable partner for a comprehensive supply of standard consumables. Guided by our dedication to deliver competent service as well as the highest quality to our customers, our company’s focus remains Peptide Chemistry, while we also have strong expertise in Drug Delivery, Life Sciences and Custom Syntheses.
Our mission is to accompany our customers in their current projects by supplying the most novel substances and latest technologies. Iris Biotech supplies Amino Acids, Resins, Reagents and Solvents. Besides that, we also offer a variety of substances for Drug Delivery, such as PEGs, both in monodisperse and in polydisperse forms, as well as various poly(amino acids), which are biodegradable alternatives to PEGs. Due to the growing demand for tailor-made compounds, we increased our Custom Synthesis capabilities.
Iris Biotech supplies Amino Acids, Resins, Reagents and Solvents. Besides that, we also offer a great variety of substances for Drug Delivery, such as PEGs, both in monodisperse and in polydisperse forms, as well as various poly(amino acids), which are biodegradable alternatives to PEGs. Both PEGs and poly(amino acids) are a popular tool for researchers to improve the solubility and pharmacokinetic properties of peptides, proteins, biopharmaceuticals and organic drug molecules. Reagents for Life Sciences and Diagnostics.
A smaller but nonetheless important part of our portfolio, the Life Sciences and Diagnostics section encompasses substrates for reporter enzymes and drug interaction studies, metabolites, glucuronides, inhibitors and inducers, antibody conjugates and cross-linkers, natural products with biological and pharmacological activity, carbohydrates, as well as dyes and fluorescent labels that are used as tools in immunology, biochemistry and molecular biology.
Irradiation of diazirines with UV light yields highly reactive intermediates that can add to neighboring molecules by irreversibly forming a covalent bond. The diazirine moiety is the smallest of all photophores, so its introduction into a peptide or protein usually does not impair its biological activity. Further advantages of diazirine crosslinkers are their stability at room temperature, as well as their relative stability to nucleophiles, and to both acidic and basic conditions.
PEGs are widely used to improve pharmacokinetic properties and resistance towards proteolytic degradation of biopharmaceuticals. They formerly were available only as polydisperse material, which makes analytics extraordinarily difficult. We here present the first monodisperse PEG derivatives of 5 kDa molecular weight which is promptly readily available and affordable. mPEG-COOH, mPEG-NH2, mPEG-N3, mPEG-SH are promptly available.
Phenol groups bearing drugs suffer rapid metabolism, resulting in low bioavailability. To overcome this handicap, we introduce an isosteric and biocompatible replacement of phenyl rings by BCP:
* isosteric replacement of phenyl
* high resistance to metabolic clearance
* already used in current APIs
* flexible and diversifiable platform
* proven biocompatibility - tested in vivo pharmacokinetic (liver & kidney)
* efficient and scalable route of synthesis suitable for commercial applications
Dr. Thomas Bruckdorfer
CSO & VP Business Development
Phone: +49 9231 97121-0
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Proteins contained in meat and other comestible goods are usually rich in the amino acids arginine and lysine. Their side chain functional groups react with reducing carbohydrates such as glucose to form Amadori reaction products. These characteristic intermediates decompose particularly at elevated temperatures to various Maillard reaction products (MRPs) which are responsible for the distinctive flavors of many food products. MRPs are widely used as markers for the nutritional quality of food and have gained broad attention in cosmetics, biochemistry, food, and pharma industry.
MRPs reduce the availability of essential amino acids such as arginine and lysine in food, and therefore influence their nutritional quality. They are responsible for deterioration of food during storage and processing. From a pharmacological point of view they may cause kidney damage and show carcinogenic, but also antiallergenic, antibiotic, anti-mutagenic, and antioxidant properties.
Phosphorylation of serine, threonine and tyrosine is counted among the most important posttranslational modifications that occur in organisms.
Therefore, the preparation of synthetic phosphorylated peptides is of significant interest for researchers. However, those synthetic efforts are frequently hampered by the lability of the phosphoester bond.
Here we present three phosphono-amino acid derivatives that serve as hydrolysis-stable mimics of pSer, pThr and pTyr, termed Pma (Ser), Pmab (Thr) and Pmp (Tyr). While those derivatives are suitably protected for their use in peptide synthesis using the Fmoc strategy, these protecting groups can be removed during final deprotection yielding phosphono-peptides, from which cellular phosphatases are unable to remove the phosphate group mimic. Consequently, peptides or semi-synthetic proteins that include Pma, Pmab or Pmp are valuable tools for cell-based experiments.