Peptide Characterization & Analytics
Analytical Methods Development
JPT is not only the peptide synthesis expert, but also conducts a wide variety of peptide analysis services to support their applications. Typical peptide analysis services include LC-MS (trap and/or quad), MALDI-MS, or HPLC. A large variety of optional analyses is available e.g. AAA, NMR, CE, sterility testing, as well as peptide content determination.
Peptides have an inherent and sequence-specific stability profile which depends on the properties of the individual peptides and their storage conditions. Chemical degradation of peptides during storage can be attributed to oxidation, hydrolysis, structural rearrangements or more. Despite this knowledge, stability of a given peptide is hard to predict. Therefore we advise for stability testing depending on the applications for short- and long-term use.
Please note that in the case certain peptides are too less stable for your application we offer peptide optimization as R&D service.
Peptide solubility is a crucial factor in nearly all peptide based projects. These include in vitro assay robustness and in vivo bioavailability. In both cases, lack of complete solubility at the desired effective concentration will lead to decreased activity and/or false negative results. A prerequisite for effective solubility assessment and optimization is the availability of a fast and sensitive solubility assay.
Turbidimetric Solubility Assay (TSA) allows a rapid determination of solubility using only small peptide amounts. Depending on applications of the target peptides, different organic and inorganic solvents and solvent additives can be applied.
Filtration through sterile membrane filters is usually the method of choice for sterilization of peptide-containing solutions. We offer our long-year experience in the optimization of filters and filtration conditions as well as screening services to develop robust a sterile filtration protocol for you project.
Due to their chemical properties lyophilized peptides may still contain traces of moisture and/or counter ions on protonated amino functions (N-terminus, Arg, His, Lys, etc.). This is not considered an impurity, but reduces the actual peptide content by approximately 10 to 30%.An accurate determination of the peptide content can be performed by quantitative amino acid analysis. The analysis includes an acidic hydrolysis of the peptide, transforming the sample into free amino acids. Then amino acid analysis and quantification of total peptide content are performed.
We are happy to offer exact sequence confirmation of peptides. Please contact us on advice what will be the optimal methodology for that.