María del Rayo Graciela Guevara-Villa

The need for storage has increased with the development of social networks and streaming platforms. The storage requirement has gone from gigabytes to zettabytes. The use of networks requires thousands of images to perform the learning that allows them to be used as classification systems in health, facilitating the diagnosis of diseases. This situation has led research centers and institutions to join the DNA Data Storage Alliance and seek new information storage strategies. As a result, it has been suggested that DNA can store data and image information innovatively due to its density, stability, and scalability. In this sense, the present work develops the necessary bioinformatics, nomenclature, and an innovative algorithm that allows storing images and video in any DNA sequence, using, as an example, the plasmid pJK635 that can be inserted into the bacterium Escherichia coli and using these plasmids as storage of image information. The results show that 2K quality images in black and white, color, and even a video sequence can be stored inside a plasmid. The developed algorithm facilitates the storage of information by converting the pixel value of the images into a sequence of DNA nucleotides that can be stored within the plasmid, including the image size information, the file type, and the set of pixels in the image, all bounded between primers. Conversely, the image can be reconstructed by passing the nucleotides to their respective pixels for display on a computer.

Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) is used to identify protein presence, absence, or overexpression and usually, their interpretation is visual. Some published methods can localize the position of proteins using image analysis on images of SDS-PAGE gels. However, they cannot automatically determine a particular protein band’s concentration or molecular weight. In this article, a new methodology to identify the number of samples present in an SDS-PAGE gel and the molecular weight of the recombinant protein is developed. SDS-PAGE images of different concentrations of pure GPN protein were created to produce homogeneous gels. Then, these images were analyzed using the developed methodology called Image Profile Based on Binarized Image Segmentation (IPBBIS). It is based on detecting the maximum intensity values of the analyzed bands and produces the segmentation of images filtered by a binary mask. The IPBBIS was developed to identify the number of samples in an SDS-PAGE gel and the molecular weight of the recombinant protein of interest, with a margin of error of 3.35%. An accuracy of 0.9850521 was achieved for homogeneous gels and 0.91736 for heterogeneous gels of low quality.

Protein purification is a complex and non-standardized process; the fact that proteins have different structural types making it difficult to create a standard methodology to obtain them in a pure, soluble, and homogeneous form. The present study shows the selective development of a buffer suitable for proteins of interest that allows high concentrations of hGPN2 protein to be obtained with low polydispersion and high homogeneity and purity. By taking the different reagents used in the construction of different buffers as a basis and performing purifications using different additives in different concentrations to determine the optimal amounts, the developed process helps to minimize the bonds, maintain solubility, release the proteins present in inclusion bodies, and provide an adequate environment for obtaining high concentrations of pure protein. GPN proteins are of unknown function, have not been purified in high concentrations, and have been found as part of the RNA polymerase assembly; if they are not expressed, the cell dies, and overexpression of certain GPN proteins has been linked to decreased survival in patients with invasive ductal carcinoma breast cancer types ER+ and HER2+. The results of the present study show that the use of the buffer developed for recombinant hGPN2 protein expressed in Escherichia coli could be manipulated in order to isolate the protein in a totally pure form and without the use of protease inhibitor tablets. The resulting homogeneity and low polydispersion was corroborated by studies carried out using dynamic dispersion analysis. Thanks to these properties, it can be used for crystallography or structural genomics studies.