Recent Studies from Auburn University Add New Data to Proteomics (Peptide Microarray with Ligands at High Density Based on Symmetrical Carrier Landscape Phage for Detection of Cellulase)
By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Proteomics. According to news reporting out of Auburn, Alabama, by NewsRx editors, research stated, "Peptide microarrays evolved recently as a routine analytical implementation in various research areas due to their unique characteristics. However, the immobilization of peptides with high density in each spot during the fabricating process remains a problem, which will affect the performance of the resultant microarray greatly."
Our news journalists obtained a quote from the research from Auburn University, "To respond to this challenge, a novel peptide immobilization method using symmetrical phage carrier was developed in this work. The cellulytic enzyme endoglucanase I (EG I) was used as a model for selection of its specific peptide ligands from the f8/8 landscape library. Three phage monoclones were selected and identified by the specificity array, of which one phage monoclone displaying the fusion peptide EGSDPRNIV (phage EGSDPRMV) could bind EG I specifically with highest affinity. Subsequently, the phage EGSDPRMV was used directly to construct peptide microarray. For comparison, major coat protein pVIII fused EG I specific peptide EGSDPRMV (pVIII-fused EGSDPRMV) which was isolated from phage EGSDPRMV was also immobilized by traditional method to fabricate peptide microarray. The fluorescent signal of the phage EGSDPRMV-mediated peptide microarray was more reproducible and about four times higher than the value for pVIII-fused EGSDPRMV-based microarray, suggesting the high efficiency of the proposed phage EGSDPRMV-mediated peptide immobilization method. Further, the phage EGSDPRMV based microarray not only simplified the procedure of microarray construction but also exhibited significantly enhanced sensitivity due to the symmetrical carrier landscape phage, which dramatically increased the density and sterical regularity of immobilized peptides in each spot."
According to the news editors, the research concluded: "Thus, the proposed strategy has the advantages that the immobilizing peptide ligands were not disturbed by their composition and the immobilized peptides were highly regular with free amino-terminal."
For more information on this research see: Peptide Microarray with Ligands at High Density Based on Symmetrical Carrier Landscape Phage for Detection of Cellulase. Analytical Chemistry, 2014;86(12):5844-5850. Analytical Chemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Analytical Chemistry - www.pubs.acs.org/journal/ancham)
Our news journalists report that additional information may be obtained by contacting H. Qi, Auburn University, Dept. of Pathobiol, Auburn, AL 36849, United States. Additional authors for this research include F. Wang, V.A. Petrenko and A.H. Liu (see also Proteomics).
Keywords for this news article include: Auburn, Alabama, United States, North and Central America, Cellulases, Enzymes and Coenzymes, Peptides, Proteins, Proteomics
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