Since sulfated peptides have different stabilities under different conditions, the efficient synthesis of sulfated peptides is technically challenging. Thanks to decades of experience in peptide modification and synthesis, CD Formulation has developed a mature sulfated peptide synthesis program that combines advanced synthesis methods and optimized reaction conditions to ensure that sulfated peptides of high purity and stability are obtained under different conditions.
Sulfation is another post-translational protein modification (PTM) of proteins and peptides. Tyrosine O-sulfation is the most common and important process for proteins and peptides and is ubiquitous in peptides and proteins of multicellular eukaryotes. The mechanism revealed by this PTM involves tyrosine protein sulfotransferase (TPST), which is responsible for the transfer of a sulfate group (-SO4) to the hydroxyl group (-OH) of tyrosine to form tyrosine-4-sulfate. Studies have shown that tyrosine O-sulfation plays an important role in enhancing protein-protein interactions and is involved in a variety of biological processes. The hydroxyl group of tyrosine is the main site of sulfation, in addition to serine (Ser) and threonine (Thr) sulphation.
Fig. 1 Tyrosine O-sulfation catalysed by TPSTs. (Stone MJ, et al., 2009)
As experts in peptide modification, CD Formulation provides unparalleled peptide sulfation services to customers around the world. We have reliable synthesis procedures and excellent peptide analysis technology to solve any possible challenges in the development and production of peptide therapeutics.
Our team of peptide experts can handle the synthesis needs of a variety of sulfated peptides listed below.
Considering the stability characteristics of tyrosine sulfated peptides, which are stable under alkaline conditions but unstable under acidic conditions. Our peptide synthesis experts have developed a mature sulfated peptide synthesis procedure and conducted in-depth research on the stability of tyrosine sulfated peptides under different pH conditions.
Amino Acid Name | Structural Formula |
Tyr(SO3H) | ![]() |
Thr(SO3H) | ![]() |
Ser(SO3H) | ![]() |
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: Preparation Methods for Peptide Thioester Containing Tyr(SO3H) Residue(s)
Journal: Chem Pharm Bull (Tokyo).
IF: 2.9
Published: 2024
Results:
The authors describe two methods for the preparation of peptide thioesters containing Tyr(SO 3 H) residues without the use of protecting groups on the sulfate moiety. Both methods are applicable to the synthesis of various types of sulfonated peptides. Method one is based on the direct thioesterification of fully protected peptide acids prepared by fluoren-9-ylmethoxycarbonyl (Fmoc) solid phase peptide synthesis (Fmoc-SPPS) on 2-chlorotrityl (Clt) resin using carbodiimide. Subsequent deprotection with trifluoroacetic acid (TFA) (0 °C, 4 h) affords peptide thioesters containing Tyr(SO 3 H) residues. Method two is based on the thioesterification of peptide azides derived from peptide hydrazides prepared by Fmoc-SPPS on NH 2 NH-Clt-resin. Peptide thioesters containing two Tyr(SO 3 H) residues prepared by this alternative approach were used as building blocks for the one-pot synthesis of the N-terminal extracellular portion of CC-chemokine receptor 5 (CCR5(9–26)) via native chemical ligation (NCL).
Fig. 2 Preparation of Peptide Thioester Containing Tyr(SO3H) Residue(s). (Sekigawa Y, et al., 2024)
CD Formulation has extensive experience with each sulfation modification of peptides. Please don't hesitate to contact us if you are interested in our services, and to learn more about the possibilities of incorporating sulfation into your peptides. We look forward to cooperating with you.
References