Catalytic antibodies and their applications in biotechnology: state of the art

Padiolleau-Lefèvre, Séverine; Naya, Raouia Ben; Shahsavarian, M.; Friboulet, Alain; Avalle, Bérangère

doi:10.1007/s10529-014-1503-8

Cited by 21 publications

(18 citation statements)

References 56 publications

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“…There are several reviews of the use of abzymes in medicine and biotechnology [ 60 , 86 , 177 , 180 , 181 , 182 ]. Certain hopes are associated with the prospect of using abzymes to treat addiction to psychoactive substances.…”

Section: The Biological Role Of Catalytic Abs and Their Use In Medmentioning

confidence: 99%

“…Certain hopes are associated with the prospect of using abzymes to treat addiction to psychoactive substances. In particular, monoclonal abzymes that hydrolyze cocaine and nicotine are being developed [ 60 , 180 ]. Abzymes that selectively hydrolyze organophosphorus compounds are beimg created.…”

Section: The Biological Role Of Catalytic Abs and Their Use In Medmentioning

confidence: 99%

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Immunoglobulins with Non-Canonical Functions in Inflammatory and Autoimmune Disease States

Ermakov

Nevinsky

Buneva

2020

IJMS

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Immunoglobulins are known to combine various effector mechanisms of the adaptive and the innate immune system. Classical immunoglobulin functions are associated with antigen recognition and the initiation of innate immune responses. However, in addition to classical functions, antibodies exhibit a variety of non-canonical functions related to the destruction of various pathogens due to catalytic activity and cofactor effects, the action of antibodies as agonists/antagonists of various receptors, the control of bacterial diversity of the intestine, etc. Canonical and non-canonical functions reflect the extreme human antibody repertoire and the variety of antibody types generated in the organism: antigen-specific, natural, polyreactive, broadly neutralizing, homophilic, bispecific and catalytic. The therapeutic effects of intravenous immunoglobulins (IVIg) are associated with both the canonical and non-canonical functions of antibodies. In this review, catalytic antibodies will be considered in more detail, since their formation is associated with inflammatory and autoimmune diseases. We will systematically summarize the diversity of catalytic antibodies in normal and pathological conditions. Translational perspectives of knowledge about natural antibodies for IVIg therapy will be also discussed.

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Section: The Biological Role Of Catalytic Abs and Their Use In Medmentioning

confidence: 99%

Section: The Biological Role Of Catalytic Abs and Their Use In Medmentioning

confidence: 99%

Immunoglobulins with Non-Canonical Functions in Inflammatory and Autoimmune Disease States

Ermakov

Nevinsky

Buneva

2020

IJMS

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“…The first antibody endowed with enzymatic properties—catalytic antibody or abzyme—was reported independently by two laboratories in 1986 . Later, based on the hypothesis that analogues mimicking the transition states of chemical reactions should be suitable haptens for the production of abzymes, several strategies were proposed to produce abzymes (Figure ) . A considerable number of abzymes have since been produced.…”

Section: Classifications Of Enzyme Mimicsmentioning

confidence: 99%

“…[110,111] Later,b ased on the hypothesis that analogues mimicking the transition states of chemicalr eactions should be suitable haptens for the production of abzymes, [112] severals trategies were proposed to produce abzymes (Figure 3). [113][114][115][116] Ac onsiderable number of abzymes have since been produced. However,t hese abzyme-productionp rocedures ( Figure 3) are rather complicated and time- consuming, owing to the complexity of the hapten designa nd complication from inhibitory antibodies.…”

Section: Nanoparticulate Enzyme Mimicsmentioning

confidence: 99%

Enzyme Mimics: Advances and Applications

Kuah

Toh

Yee

et al. 2016

Chemistry A European J

277

151

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Enzyme mimics or artificial enzymes are a class of catalysts that have been actively pursued for decades and have heralded much interest as potentially viable alternatives to natural enzymes. Aside from having catalytic activities similar to their natural counterparts, enzyme mimics have the desired advantages of tunable structures and catalytic efficiencies, excellent tolerance to experimental conditions, lower cost, and purely synthetic routes to their preparation. Although still in the midst of development, impressive advances have already been made. Enzyme mimics have shown immense potential in the catalysis of a wide range of chemical and biological reactions, the development of chemical and biological sensing and anti-biofouling systems, and the production of pharmaceuticals and clean fuels. This Review concerns the development of various types of enzyme mimics, namely polymeric and dendrimeric, supramolecular, nanoparticulate and proteinic enzyme mimics, with an emphasis on their synthesis, catalytic properties and technical applications. It provides an introduction to enzyme mimics and a comprehensive summary of the advances and current standings of their applications, and seeks to inspire researchers to perfect the design and synthesis of enzyme mimics and to tailor their functionality for a much wider range of applications.

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“…Antibodies generated by immunizing an animal with a putative transition-state analog (TSA) of the chemical reaction are expected to possess antigen-combining sites to be both geometrically and electronically complementary to the transition state of the reaction and to successfully catalyze the chemical reaction [ 1 , 2 ]. These catalytic antibodies have attracted wide attention as possible tailor-made catalysts for chemical transformations, and have been used in biotechnology and in clinical applications [ 3 ]. The catalytic antibodies 6D9, 9C10, and 7C8 were induced by immunization with a phosphonate TSA 3 , designed on the basis of the stabilization of transition state 4 ; these antibodies catalyzed the hydrolysis of a nonbioactive chloramphenicol monoester derivative 1 to generate a bioactive chloramphenicol 2 ( Fig.…”

mentioning

confidence: 99%

Effects of substrate conformational strain on binding kinetics of catalytic antibodies

2016

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We analyzed the correlation between the conformational strain and the binding kinetics in antigen-antibody interactions. The catalytic antibodies 6D9, 9C10, and 7C8 catalyze the hydrolysis of a nonbioactive chloramphenicol monoester derivative to generate a bioactive chloramphenicol. The crystal structure of 6D9 complexed with a transition-state analog (TSA) suggests that 6D9 binds the substrate to change the conformation of the ester moiety to a thermodynamically unstable twisted conformation, enabling the substrate to reach the transition state during catalysis. The present binding kinetic analysis showed that the association rate for 6D9 binding to the substrate was much lower than that to TSA, whereas those for 9C10 and 7C8 binding were similar to those to TSA. Considering that 7C8 binds to the substrate with little conformational change in the substrate, the slow association rate observed in 6D9 could be attributed to the conformational strain in the substrate.

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Catalytic antibodies and their applications in biotechnology: state of the art

Cited by 21 publications

References 56 publications

Immunoglobulins with Non-Canonical Functions in Inflammatory and Autoimmune Disease States

Immunoglobulins with Non-Canonical Functions in Inflammatory and Autoimmune Disease States

Enzyme Mimics: Advances and Applications

Effects of substrate conformational strain on binding kinetics of catalytic antibodies

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