Selective Enrichment Of Peptides Research Articles

Hypoallergenic hydrolysates of egg white proteins modulate allergen responses induced ex vivo on spleen cells from sensitized mice

This study describes the in vivo allergenicity of enzymatic hydrolysates of egg white proteins (ovalbumin, lysozyme and ovomucoid) and explores the possibility that they could modulate T cell cytokine responses to egg allergens ex vivo, using splenocytes from BALB/c mice sensitized to individual egg proteins or to their mixtures in different proportions. The hydrolysate of ovalbumin with pepsin could be regarded as a good candidate for peptide-based immunotherapy on the grounds of its reduced ability to trigger allergic symptoms in a passive cutaneous anaphylaxis assay and its potential to reduce Th2 responses (release of IL-4 and IL-5) induced by egg allergens in the spleen cell cultures, but also to enhance Th1 responses (release of TNF-α and IFN-γ). While it is possible to obtain chromatographic fractions containing peptides with different Th2-inhibiting or promoting properties, as judged by cytokine production, selective peptide enrichment did not lead to an increase in the immunomodulating efficiency as compared with the whole ovalbumin hydrolysate, possibly due to the presence in the latter of a combination of immunogenic peptides with synergistic or adjuvant actions.

Salivary Peptidomic Analysis -The Extension of Proteomics

Nowadays, proteomic-related studies have developed rapidly and improvement has been made in the scientific and technological fields. Besides the proteome, the peptidome with low molecular weight has apparently attracted increasing attention in recent years too. The peptidome performs a large array of vital biological functions to contribute to homeostasis in the certain tissues. However, due to the interference by high-abundance proteins in complex biological body fluids such as saliva and serum, selective enrichment of peptides with low molecular weight is the first and most important step before analyzing the peptidome. This review mainly illustrates the general concept of the peptidome, specific methods of saliva collection, advanced peptidomic technologies and the recently developed peptidomic-related reports, as well as some limitations of the application in salivary peptidome. The future prospects of the peptidome are also involved.

Functionalized Periodic Mesoporous Organosilicas for Enhanced and Selective Peptide Enrichment

The analysis of peptides by the mass spectrometry (MS) technique is important in modern life science. The enrichment of peptides can increase the detection efficiency and is sometimes indispensable for collecting the information on proteins with low-abundance. Herein, we first report that functionalized periodic mesoporous organosilica (PMO) materials have a superior peptide enrichment property. It is demonstrated that the PMO materials with an organo-bridged (-CH(2)-) hybrid wall composition display a highly enhanced peptide enrichment ability compared to the pure silica material (SBA-15) with similar mesostructured parameters and morphology. More importantly, by surface modification of PMO with amino groups (denoted NH(2)-PMO), PMO and NH(2)-PMO with opposite charged surfaces (-25.2 and +39.0 mV, respectively) show selective affinities for positively and negatively charged peptides, respectively. By directly adding PMO, NH(2)-PMO as well as pure silica materials to the peptides solution with a low concentration (1-2 fmol/microL), 36 and 28 peptides can be detected from the BSA digestion in the presence of PMO and NH(2)-PMO, respectively, while only 6 and 4 are monitored in the case of SBA-15 enrichment and from solution without enrichment, respectively. Moreover, 69.4% (25 of 36) of enriched peptides by PMO have pI > or = 6 and 80% (21 of 28) of enriched peptides by NH(2)-PMO possess pI < or = 6. Combining the results from the NH(2)-PMO and PMO enrichment together, 51 peptides can be identified with a MOWSE score of 333. It is also noted that similar conclusions can also be obtained from the peptides solution originated from other proteins. This might be an important contribution to the understanding of the interaction between peptides and porous hosts, and the proposed method is promising for the development of both material science and biotechnology.