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The mysterious duality of DNA: What is the difference between deoxyribase and RNase?
In biological systems, enzymes are important molecules that facilitate chemical reactions. Although we usually focus on protein enzymes and RNases, in recent years, deoxyribozymes have gradually surfaced and become a hot topic in scientific research.
Deoxyribase, also known as DNase, is a DNA oligonucleotide that can carry out specific chemical reactions. Meanwhile, the role of RNases and proteinases as biocatalysts has long been known. Research on deoxyribase has revealed the essential differences in the catalytic activities of DNA and RNA, which has given us a deeper understanding of these two nucleic acids.
The chemical activity of deoxyribase is weaker than that of RNase and proteinase in many cases.
The rarity of deoxyribase is closely related to its chemical structure. DNA is composed of four chemically similar bases, which allows it to perform only a limited number of interactions in catalytic reactions, such as hydrogen bonding, π stacking and metal ion coordination. In contrast, proteins are composed of up to twenty different amino acids, which gives them greater catalytic properties and diversity. What's more, the structure of DNA usually exists in the form of a double helix, which would limit its physical flexibility and ability to form three-dimensional structures.
Since 1994, scientists have begun to explore and synthesize deoxyribozymes with catalytic activity. Taking GR-5 as an example, it can catalyze the cleavage of phosphate bonds, showing a catalytic efficiency that is 100 times higher than that of uncatalyzed reactions. Since then, the scientific community has discovered several other deoxyribozymes that can synergize with metal coenzymes, including Mg2+-dependent E2 deoxyribase and Ca2+-dependent Mg5 deoxyribase.
To have a deeper understanding of the functions of deoxyribozymes, we first need to understand that they are significantly different from RNases and protein enzymes in structure and catalytic mechanism.
In addition, the selectivity of deoxyribase also shows special chemical selectivity. Specific deoxyribozymes have a high affinity for certain metal coenzymes such as Pb2+ or sodium ions, which is especially prominent when performing RNA grafting reactions. This type of deoxyribase-based catalytic reaction and its potential in virus suppression, tumor treatment and other applications make it one of the potential therapies.
Applications of deoxyribase
The application range of deoxyribase is quite wide. Research into treatments for asthma, ulcerative colitis and certain cancers is advancing in clinical trials. Research shows that SB010, a specially designed deoxyribase, can effectively inhibit the transcription factor GATA-3 of a specific signaling pathway, showing good efficacy and safety in trials conducted under the guidance of nurses.
Using deoxyribozymes to transcribe and target specific mRNA may be the key to future biomedicine.
In addition, deoxyribozymes also show potential in areas such as environmental detection and biological imaging. For example, deoxyribase has been used in the past to detect lead ions in water, showing its potential as a metal biosensor.
Differences from RNase
Compared with RNase, the advantages of deoxyribase are cost-effectiveness, synthesis accuracy and sequence length. The development of RNase began in the 1980s, but the development of DNase and its flexibility in chemical synthesis have demonstrated its uniqueness. For example, when some DNA catalysts undergo asymmetric synthesis, changing their structures according to different reaction conditions can effectively improve their catalytic effect.
Although the current mainstream catalysts are mostly protein and RNA stretchers, the birth of deoxyribase has made us rethink the catalytic potential of nucleic acids and how this potential will affect future biomedicine and synthetic chemistry.
We should probably think about how the study of deoxyribozymes will change our understanding of biocatalysis and nucleic acids?
