Mirror life (also called mirror-image life) is a hypothetical form of life with mirror-reflected molecular building blocks. [1] [2] [3] [4] [5] The possibility of mirror life was first discussed by Louis Pasteur. [6] This alternative life form has never been discovered in nature, but efforts to build a mirror-image version of biology's molecular machinery are underway. [7]
In December 2024, a broad coalition of scientists, including leading synthetic biology researchers and Nobel laureates, warned that the creation of mirror life, including mirror bacteria, could cause "unprecedented and irreversible harm" to human health and ecosystems worldwide. [8] [9] Its potential to escape immune defenses and invade natural ecosystems might lead to "pervasive lethal infections in a substantial fraction of plant and animal species, including humans." Given these risks, the scientists concluded that mirror organisms should not be created without compelling evidence of safety. [8]
Many of the essential molecules for life on Earth can exist in two mirror-image forms, often called "left-handed" and "right-handed", where handedness refers to the direction in which polarized light skews when beamed through a pure solution of the molecule, but living organisms do not use both. [10] RNA and DNA contain only right-handed sugars; proteins are exclusively composed of left-handed amino acids, although many bacteria and fungi are able to synthesise non-ribosomal peptides containing right-handed amino acids, as the example of peptidoglycan synthesis shows. This phenomenon is known as homochirality. [11] It is not known whether homochirality emerged before or after life, whether the building blocks of life must have this particular chirality, or indeed whether life needs to be homochiral. [12] Protein chains built from amino acids of mixed chirality tend not to fold or function well, but mirror-image proteins have been constructed that have identical function but on substrates of opposite handedness. [11]
Advances in synthetic biology, like synthesizing viruses since 2002, partially synthetic bacteria in 2010, and synthetic ribosomes in 2013, may lead to the possibility of fully synthesizing a living cell from small molecules, which could enable synthesizing mirror cells from mirrored versions (enantiomers) of life's building-block molecules. Some proteins have been synthesized in mirror-image versions, including polymerase in 2016. [13] [14]
Reconstructing regular lifeforms in mirror-image form, using the mirror-image (chiral) reflection of their cellular components, could be achieved by substituting left-handed amino acids with right-handed ones, in order to create mirror reflections of proteins, and likewise substituting right-handed with left-handed nucleic acids. [15] Because the phospholipids of cell membranes are also chiral, American geneticist George Church proposed using an achiral fatty acid instead of mirror-image phospholipids for the membrane. [15]
Electromagnetic force (chemistry) is unchanged under such molecular reflection transformation (P-symmetry). There is a small alteration of weak interactions under reflection, which can produce very small corrections that theoretically favor the natural enantiomers of amino acids and sugars, [16] but it is unknown if this effect is large enough to affect the functionality of mirror biomolecules or explain homochirality in nature. [17]
Mirror animals would need to feed on reflected food, produced by reflected plants. Mirror viruses would not be able to attack natural cells, just as natural viruses would not be able to attack mirror cells. [15]
Mirror life presents potential dangers. For example, a chiral-mirror version of cyanobacteria, which only needs achiral nutrients and light for photosynthesis, could take over Earth's ecosystem due to lack of natural enemies, disturbing the bottom of the food chain by producing mirror versions of the required sugars. [15] Some bacteria can digest L-Glucose; exceptions like this would give some rare lifeforms an unanticipated advantage.
Direct application of mirror-chiral organisms can be mass production of enantiomers (mirror-image) of molecules produced by normal life.
The creation of a mirror human is the basis of the 1950 short story "Technical Error" by Arthur C. Clarke. [21] In this story, a physical accident transforms a person into his mirror image, speculatively explained by travel through a fourth physical dimension. H. G. Wells' The Plattner Story (1896) is based on a similar idea.
In the 1970 Star Trek novel Spock Must Die! by James Blish, the science officer of the USS Enterprise is replicated in mirror form by a transporter mishap. He locks himself in the sick bay where he is able to synthesize mirror forms of basic nutrients needed for his survival. [22]
An alien machine that reverses chirality, and a blood-symbiont that functions properly only when in one chirality, were central to Roger Zelazny's 1976 novel Doorways in the Sand . [23]
On the titular planet of Sheri S. Tepper's 1989 novel Grass , some lifeforms have evolved to use the right-handed isomer of alanine. [24]
In the Mass Effect series, chirality of amino acids in foodstuffs is discussed often in both dialogue and encyclopedia files.
In the 2014 science fiction novel Cibola Burn by James S. A. Corey, the planet Ilus has indigenous life with partially-mirrored chirality. This renders human colonists unable to digest native flora and fauna, and greatly complicates conventional farming. Consequently, the colonists have to rely upon hydroponic farming and food importation. [25]
In the 2017 Daniel Suarez novel Change Agent, an antagonist, Otto, nicknamed the "Mirror Man", is revealed to be a genetically-engineered mirror human. He views other humans with disdain and causes them to feel an inexplicable repulsion by his very presence. [26]
The concept is used during Ryan North's 2023 run on Fantastic Four as an existential threat towards the human population. [27]
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life.
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology, and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, in turn relating greatly to the understanding of tissues and organs as well as organism structure and function. Biochemistry is closely related to molecular biology, the study of the molecular mechanisms of biological phenomena.
Metabolism is the set of life-sustaining chemical reactions in organisms. The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks of proteins, lipids, nucleic acids, and some carbohydrates; and the elimination of metabolic wastes. These enzyme-catalyzed reactions allow organisms to grow and reproduce, maintain their structures, and respond to their environments. The word metabolism can also refer to the sum of all chemical reactions that occur in living organisms, including digestion and the transportation of substances into and between different cells, in which case the above described set of reactions within the cells is called intermediary metabolism.
In chemistry, a racemic mixture or racemate is one that has equal amounts of left- and right-handed enantiomers of a chiral molecule or salt. Racemic mixtures are rare in nature, but many compounds are produced industrially as racemates.
Proteinogenic amino acids are amino acids that are incorporated biosynthetically into proteins during translation. The word "proteinogenic" means "protein creating". Throughout known life, there are 22 genetically encoded (proteinogenic) amino acids, 20 in the standard genetic code and an additional 2 that can be incorporated by special translation mechanisms.
In chemistry, racemization is a conversion, by heat or by chemical reaction, of an optically active compound into a racemic form. This creates a 1:1 molar ratio of enantiomers and is referred to as a racemic mixture. Plus and minus forms are called Dextrorotation and levorotation. The D and L enantiomers are present in equal quantities, the resulting sample is described as a racemic mixture or a racemate. Racemization can proceed through a number of different mechanisms, and it has particular significance in pharmacology as different enantiomers may have different pharmaceutical effects.
In chemistry, a molecule or ion is called chiral if it cannot be superposed on its mirror image by any combination of rotations, translations, and some conformational changes. This geometric property is called chirality. The terms are derived from Ancient Greek χείρ (cheir) 'hand'; which is the canonical example of an object with this property.
Xenobiology (XB) is a subfield of synthetic biology, the study of synthesizing and manipulating biological devices and systems. The name "xenobiology" derives from the Greek word xenos, which means "stranger, alien". Xenobiology is a form of biology that is not (yet) familiar to science and is not found in nature. In practice, it describes novel biological systems and biochemistries that differ from the canonical DNA–RNA-20 amino acid system. For example, instead of DNA or RNA, XB explores nucleic acid analogues, termed xeno nucleic acid (XNA) as information carriers. It also focuses on an expanded genetic code and the incorporation of non-proteinogenic amino acids, or “xeno amino acids” into proteins.
Homochirality is a uniformity of chirality, or handedness. Objects are chiral when they cannot be superposed on their mirror images. For example, the left and right hands of a human are approximately mirror images of each other but are not their own mirror images, so they are chiral. In biology, 19 of the 20 natural amino acids are homochiral, being L-chiral (left-handed), while sugars are D-chiral (right-handed). Homochirality can also refer to enantiopure substances in which all the constituents are the same enantiomer, but some sources discourage this use of the term.
Ronald Charles David Breslow was an American chemist from Rahway, New Jersey. He was University Professor at Columbia University, where he was based in the Department of Chemistry and affiliated with the Departments of Biological Sciences and Pharmacology; he had also been on the faculty of its Department of Chemical Engineering. He had taught at Columbia since 1956 and was a former chair of the university's chemistry department.
In chemistry, absolute configuration refers to the spatial arrangement of atoms within a molecular entity that is chiral, and its resultant stereochemical description. Absolute configuration is typically relevant in organic molecules where carbon is bonded to four different substituents. This type of construction creates two possible enantiomers. Absolute configuration uses a set of rules to describe the relative positions of each bond around the chiral center atom. The most common labeling method uses the descriptors R or S and is based on the Cahn–Ingold–Prelog priority rules. R and S refer to rectus and sinister, Latin for right and left, respectively.
Racemic crystallography is a technique used in structural biology where crystals of a protein molecule are developed from an equimolar mixture of an L-protein molecule of natural chirality and its D-protein mirror image. L-protein molecules consist of 'left-handed' L-amino acids and the achiral amino acid glycine, whereas the mirror image D-protein molecules consist of 'right-handed' D-amino acids and glycine. Typically, both the L-protein and the D-protein are prepared by total chemical synthesis.
An enantiopure drug is a pharmaceutical that is available in one specific enantiomeric form. Most biological molecules are present in only one of many chiral forms, so different enantiomers of a chiral drug molecule bind differently to target receptors. Chirality can be observed when the geometric properties of an object is not superimposable with its mirror image. Two forms of a molecule are formed from a chiral carbon, these two forms are called enantiomers. One enantiomer of a drug may have a desired beneficial effect while the other may cause serious and undesired side effects, or sometimes even beneficial but entirely different effects. The desired enantiomer is known as an eutomer while the undesired enantiomer is known as the distomer. When equal amounts of both enantiomers are found in a mixture, the mixture is known as a racemic mixture. If a mixture for a drug does not have a 1:1 ratio of its enantiomers it is a candidate for an enantiopure drug. Advances in industrial chemical processes have made it economical for pharmaceutical manufacturers to take drugs that were originally marketed as a racemic mixture and market the individual enantiomers, either by specifically manufacturing the desired enantiomer or by resolving a racemic mixture. On a case-by-case basis, the U.S. Food and Drug Administration (FDA) has allowed single enantiomers of certain drugs to be marketed under a different name than the racemic mixture. Also case-by-case, the United States Patent Office has granted patents for single enantiomers of certain drugs. The regulatory review for marketing approval and for patenting is independent, and differs country by country.
Chirality is a property of asymmetry important in several branches of science. The word chirality is derived from the Greek χείρ (kheir), "hand", a familiar chiral object.
An L-ribonucleic acid aptamer is an RNA-like molecule built from L-ribose units. It is an artificial oligonucleotide named for being a mirror image of natural oligonucleotides. L-RNA aptamers are a form of aptamers. Due to their L-nucleotides, they are highly resistant to degradation by nucleases. L-RNA aptamers are considered potential drugs and are currently being tested in clinical trials.
l-Photo-leucine is a synthetic derivative of the l-leucine amino acid that is used as its natural analog and is characterized for having photo-reactivity, which makes it suitable for observing and characterizing protein-protein interactions (PPI). When a protein containing this amino acid (A) is exposed to ultraviolet light while interacting with another protein (B), the complex formed from these two proteins (AB) remains attached and can be isolated for study.
D-Amino acids are amino acids where the stereogenic carbon alpha to the amino group has the D-configuration. For most naturally-occurring amino acids, this carbon has the L-configuration. D-Amino acids are occasionally found in nature as residues in proteins. They are formed from ribosomally-derived D-amino acid residues.
Ribose is a simple sugar and carbohydrate with molecular formula C5H10O5 and the linear-form composition H−(C=O)−(CHOH)4−H. The naturally occurring form, d-ribose, is a component of the ribonucleotides from which RNA is built, and so this compound is necessary for coding, decoding, regulation and expression of genes. It has a structural analog, deoxyribose, which is a similarly essential component of DNA. l-ribose is an unnatural sugar that was first prepared by Emil Fischer and Oscar Piloty in 1891. It was not until 1909 that Phoebus Levene and Walter Jacobs recognised that d-ribose was a natural product, the enantiomer of Fischer and Piloty's product, and an essential component of nucleic acids. Fischer chose the name "ribose" as it is a partial rearrangement of the name of another sugar, arabinose, of which ribose is an epimer at the 2' carbon; both names also relate to gum arabic, from which arabinose was first isolated and from which they prepared l-ribose.
Viedma ripening or attrition-enhanced deracemization is a chiral symmetry breaking phenomenon observed in solid/liquid mixtures of enantiomorphous crystals that are subjected to comminution. It can be classified in the wider area of spontaneous symmetry breaking phenomena observed in chemistry and physics.
A D-peptide is a small sequence of D-amino acids. Since ribosomes are specific to L-amino acids, D-peptides rarely occur naturally in organisms and are not easily digested or degraded. D-peptide peptidomimetics are D-peptides designed to mimic natural L-peptides that commonly have therapeutic properties. A peptide with secondary structure cannot be mimicked by its retro-inverse, as linking in the reverse order breaks many backbone interactions essential for the secondary structure. An approach to mimicking these peptides is by searching for similar (sidechain) structures in a mirrored copy of the Protein Data Bank for the structured elements, and then linking the sections by retro-inversed versions of the loops found in the original protein.