Although information is ubiquitous, and its technology arguably among the highest that humankind has produced, its very ubiquity has posed new types of problems. Three that involve storage of information (rather than computation) include its usage of energy, the robustness of stored information over long times, and its ability to resist corruption through tampering. The difficulty in solving these problems using present methods has stimulated interest in the possibilities available through fundamentally different strategies, including storage of information in molecules. Here we show that storage of information in mixtures of readily available, stable, low-molecular-weight molecules offers new approaches to this problem. This procedure uses a common, small set of molecules (here, 32 oligopeptides) to write binary information. It minimizes the time and difficulty of synthesis of new molecules. It also circumvents the challenges of encoding and reading messages in linear macromolecules. We have encoded, written, stored, and read a total of approximately 400 kilobits (both text and images), coded as mixtures of molecules, with greater than 99% recovery of information, written at an average rate of 8 bits/s, and read at a rate of 20 bits/s. This demonstration indicates that organic and analytical chemistry offer many new strategies and capabilities to problems in long-term, zero-energy, robust information storage.
The rapidly increasing use of digital technologies requires the rethinking of methods to store data. This work shows that digital data can be stored in mixtures of fluorescent dye molecules, which are deposited on a surface by inkjet printing, where an amide bond tethers the dye molecules to the surface. A microscope equipped with a multichannel fluorescence detector distinguishes individual dyes in the mixture. The presence or absence of these molecules in the mixture encodes binary information (i.e., “0” or “1”). The use of mixtures of molecules, instead of sequence-defined macromolecules, minimizes the time and difficulty of synthesis and eliminates the requirement of sequencing. We have written, stored, and read a total of approximately 400 kilobits (both text and images) with greater than 99% recovery of information, written at an average rate of 128 bits/s (16 bytes/s) and read at a rate of 469 bits/s (58.6 bytes/s).
Laundry detergent formulations include proteases to digest and clean protein-based stains. Methods that can profile protease activity and specificity in detergents could be important in guiding the development of engineered proteases for these applications. The work reported here uses peptide arrays with analysis by self-assembled monolayers for matrix-assisted laser desorption/ionization (SAMDI) mass spectrometry to analyze protease activity across a 324-peptide library for five commercial laundry detergents. The results showed differences in cleavage activity across different brands. The combination of peptide arrays and SAMDI mass spectrometry provides a rapid and reliable technique for analyzing protease activities in laundry detergents and has the potential to play an important role in the development of new proteases and detergent formulations.
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