Nanotechnology in proteomics: current status, promises and challenges

In genomics, the ability to amplify rare transcripts has enabled rapid advances in the understanding of gene expression patterns in human disease. The inability to increase the copy number and to detect the signal of rare proteins as unique species in biological samples has hindered the ability of proteomics to dissect human disease with the same complexity as genomic analyses. Advances in nanotechnology have begun to allow researchers to identify low-abundance proteins in samples through techniques that rely upon both nanoparticles and nanoscale devices. This review describes some of the physical and chemical principles underlying nanomaterials and devices and outlines how they can be used in proteomics; developments which are establishing nanoproteomics as a new field. Nanoproteomics will provide the platform for the discovery of next generation biomarkers. The most promising candidates for nanoproteomics, namely carbon nanotubes and nanowires, quantum dots and nanoscopic gold particles, offer several advantages such as high sensitivity, real-time measurements and improved reproducibility

study on the activity and thermal stability of adenosine deaminase in the presence of spermine

Adenosine Deaminase is an amino hydrolase [EC 3.5.4.4] which participates in the purine metabolism where it degrades either adenosine or 2'-deoxyadenosine producing inosine or 2'- deoxy inosine, respectively. The enzyme contains a parallel alpha/beta -barrel motif with eight central beta strands and eight peripheral alpha helices. ADA is located both in the cytosol and on the cell membrane. Since spermine, a natural metabolite, exists in all cells and tissues and its effect on the cell proliferation and enzyme regulation have been reported, thermal inactivation of the ADA and spermine regulatory effect on the ADA activity have been investigated in this study. Percentage of ADA activity in the presence and absence of spermine [1000 microM] in Tris buffer 50 mM, pH 7.5 at physiologic and pathologic temperatures have been reported in the present study. Thermal inactivation curves for ADA in the absence and presence of spermine [1000 microM] in different temperatures ranging from 55 degreeC to 70 degreeC have been drawn. Our data showed that spermine activates the enzyme in the low concentrations of adenosine at 37 degreeC. However, it inhibits ADA activity at 42 degreeC in the same concentrations of substrate. It is concluded that spermine regulatory effect depends on combined influence of temperature and adenosine concentration. Furthermore, thermal stability of the enzyme also depends on temperature in presence of spermine. Binding site of spermine on the enzyme has been identified by docking analysis