Creative Peptides has unique expertise in determining the disulfide bridges of peptide, which can analyze the structure and function of peptide in multiple samples from different sources.
The physiological and pathological relevance of disulfide bridges to diseases and protein functions has been increasingly recognized, such as tumor immunity, hemostasis, cell death, and neurodegenerative diseases, etc.
Therefore, the analysis of disulfide bridges in peptides/proteins is of great significance for revealing their structure and biological functions, as well as for peptide characterization and peptide drug development in the production process of biopharmaceuticals.
We use a peptide map-based strategy to identify the number and location of disulfide bridges and free thiols. Analysis usually includes digestion with appropriate enzymes and/or chemicals, and inspection of the resulting compounds using liquid chromatography-mass spectrometry (LC-MS) and/or LC/ESI-MS/MS to separate and identify potential disulfide bridged peptides.
According to the availability and quantity of protein samples and customer requirements, we provide two different types of disulfide bridges determination services.
| Service | Method | Application |
| Analytical Disulfide Bridges Determination | The analysis is carried by an LC-MS system with both a UV-Visible detector and an MS detector. The quantitation of free or disulfide-linked peptides is based on HPLC chromatography. | Used to determine the number, the position and ratio of disulfide bridges linkages in a peptide. |
| Micro Disulfide Bridges Determination | The analysis is carried out on a Nano LC-ESI-MS/MS system without a UV-visible detector. | Often used for research stage peptide samples that the disulfide linkage is unknown |
The technical reports we provide include experimental procedures, liquid chromatography, and mass spectrometer parameters, MS raw data files, peptide identification and strength, disulfide bridges maps, and bioinformatics analysis.
Identification by mass spectrometry requires enough pure samples to obtain good data. Therefore, it is important to prepare samples in a clean laboratory to avoid contamination.
Samples can be submitted in liquid or lyophilized form.
Contact us today to find out more about our disulfide bridge analysis.
Disulfide bridges play a critical role in the stability and function of peptides and proteins. Analyzing them helps reveal the structure-function relationship and is essential for understanding peptide interactions in biological systems.
We use a peptide map-based strategy combining liquid chromatography-mass spectrometry (LC-MS) and/or LC/ESI-MS/MS. This allows for the identification and quantification of disulfide bridges and free thiols in peptides.
Analyzing disulfide bridges provides detailed structural information that is vital for peptide characterization, quality control, and process optimization during peptide synthesis.
The analytical method uses LC-MS with both UV and MS detectors, ideal for determining the number and position of disulfide bonds. The micro method utilizes Nano LC-ESI-MS/MS, often used in research stages for peptide samples with unknown disulfide linkages.
For accurate results, samples should be pure (≥ 90% purity) and free from contaminants. Peptides should be submitted in liquid or lyophilized form, stored appropriately during transport to maintain stability.
Our reports include detailed experimental procedures, LC-MS and MS raw data files, peptide identification, disulfide bridge maps, and bioinformatics analysis, all crucial for thorough structural analysis.
Yes, we offer the option to combine disulfide bridge analysis with other services like peptide sequencing or purity analysis, providing a comprehensive view of your peptide's structure and functionality.
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