Highly Regioselective Synthesis of 3′-O-Acyl-Trifluridines Catalyzed by Pseudomonas cepacia Lipase

Wang, Zhao-Yu; Bi, Yanhong; Zong, Min‐Hua

doi:10.1007/s12010-011-9333-9

Cited by 12 publications

(6 citation statements)

References 27 publications

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“…However, TFT presents the same problems as FUdR and other nucleoside drugs. As an alternative, Wang, Bi, and Zong () proposed the enzymatic synthesis of 3′‐O‐Acyl‐trifluridines. This prodrug was obtained using Lipase PS‐D to catalyze the acylation of TFT with different vinyl esters.…”

Section: Synthesis Of Drugsmentioning

confidence: 99%

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Sánchez

Tonetto

Ferreira

2017

Biotech & Bioengineering

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The lipase from Burkholderia cepacia, formerly known as Pseudomonas cepacia lipase, is a commercial enzyme in both soluble and immobilized forms widely recognized for its thermal resistance and tolerance to a large number of solvents and short-chain alcohols. The main applications of this lipase are in transesterification reactions and in the synthesis of drugs (because of the properties mentioned above). This review intends to show the features of this enzyme and some of the most relevant aspects of its use in different synthesis reactions. Also, different immobilization techniques together with the effect of various compounds on lipase activity are presented. This lipase shows important advantages over other lipases, especially in reaction media including solvents or reactions involving short-chain alcohols.

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Section: Synthesis Of Drugsmentioning

confidence: 99%

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Sánchez

Tonetto

Ferreira

2017

Biotech & Bioengineering

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“…Particularly for T. lanuginosus lipase, the immobilized supports, including Fe 3 O 4 -PDA and granulated silica, did not change the enzyme's selectivity toward the OH position. In the acylation of polyhydroxy nucleosides reported by Li and our group (Li et al, 2009a;Wang et al, 2011), however, TLIM was been found to be superior to other enzymes when it came to functionalizing its favorable secondary hydroxyl group. X-ray crystallographic studies have shown that the amphiphilic active center of TLL contains a large hydrophobic acyl chain-binding groove and a smaller hydrophilic pocket in which the alcohol moiety and Tyr 21 bind (Noinville et al, 2002).…”

Section: Influence Of Enzyme Sourcementioning

confidence: 88%

Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

Wang

et al. 2021

Front. Bioeng. Biotechnol.

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The conversion of flavonoid glycosides and their analogs to their lipophilic ester derivatives was developed by nanobiocatalysts from immobilizing Thermomyces lanuginosus lipase (TLL) on polydopamine-functionalized magnetic Fe3O4 nanoparticles (Fe3O4-PDA-TLL). The behavior investigation revealed that Fe3O4-PDA-TLL exhibits a preference for long chain length fatty acids (i.e., C10 to C14) with higher reaction rates of 12.6–13.9 mM/h. Regarding the substrate specificity, Fe3O4-PDA-TLL showed good substrate spectrum and favorably functionalized the primary OH groups, suggesting that the steric hindrances impeded the secondary or phenolic hydroxyl groups of substrates into the bonding site of the active region of TLL to afford the product.

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“…Lipase-mediated acylation of nucleosides has also been performed to increase their lipophilicity. For example, Wang et al ( 52 ) described the regioselective acylation of 21a catalyzed by immobilized PSL-C employing vinyl esters as acyl donors to obtain 3- O -acyl derivatives with improved pharmacokinetic properties.…”

Section: Biocatalyzed Synthesis Of Nucleosides and Nucleotides With A...mentioning

confidence: 99%

Biocatalyzed Synthesis of Glycostructures with Anti-infective Activity

et al. 2022

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Conspectus Molecules containing carbohydrate moieties play essential roles in fighting a variety of bacterial and viral infections. Consequently, the design of new carbohydrate-containing drugs or vaccines has attracted great attention in recent years as means to target several infectious diseases. Conventional methods to produce these compounds face numerous challenges because their current production technology is based on chemical synthesis, which often requires several steps and uses environmentally unfriendly reactants, contaminant solvents, and inefficient protocols. The search for sustainable processes such as the use of biocatalysts and eco-friendly solvents is of vital importance. Therefore, their use in a variety of reactions leading to the production of pharmaceuticals has increased exponentially in the last years, fueled by recent advances in protein engineering, enzyme directed evolution, combinatorial biosynthesis, immobilization techniques, and flow biocatalysis. In glycochemistry and glycobiology, enzymes belonging to the families of glycosidases, glycosyltransferases (Gtfs), lipases, and, in the case of nucleoside and nucleotide analogues, also nucleoside phosphorylases (NPs) are the preferred choices as catalysts. In this Account, on the basis of our expertise, we will discuss the recent biocatalytic and sustainable approaches that have been employed to synthesize carbohydrate-based drugs, ranging from antiviral nucleosides and nucleotides to antibiotics with antibacterial activity and glycoconjugates such as neoglycoproteins (glycovaccines, GCVs) and glycodendrimers that are considered as very promising tools against viral and bacterial infections. In the first section, we will report the use of NPs and N -deoxyribosyltransferases for the development of transglycosylation processes aimed at the synthesis of nucleoside analogues with antiviral activity. The use of deoxyribonucleoside kinases and hydrolases for the modification of the sugar moiety of nucleosides has been widely investigated. Next, we will describe the results obtained using enzymes for the chemoenzymatic synthesis of glycoconjugates such as GCVs and glycodendrimers with antibacterial and antiviral activity. In this context, the search for efficient enzymatic syntheses represents an excellent strategy to produce structure-defined antigenic or immunogenic oligosaccharide analogues with high purity. Lipases, glycosidases, and Gtfs have been used for their preparation. Interestingly, many authors have proposed the use Gtfs originating from the biosynthesis of natural glycosylated antibiotics such as glycopeptides, macrolides, and aminoglycosides. These have been used in the chemoenzymatic semisynthesis of novel antibiotic derivatives by modification of the sugar moiety linked to their complex scaffold. These contributions will be described in the last section of this review because of their relevance in the fight against the spreading ph...

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Highly Regioselective Synthesis of 3′-O-Acyl-Trifluridines Catalyzed by Pseudomonas cepacia Lipase

Cited by 12 publications

References 27 publications

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Burkholderia cepacia lipase: A versatile catalyst in synthesis reactions

Immobilized Fe3O4-Polydopamine-Thermomyces lanuginosus Lipase-Catalyzed Acylation of Flavonoid Glycosides and Their Analogs: An Improved Insight Into Enzymic Substrate Recognition

Biocatalyzed Synthesis of Glycostructures with Anti-infective Activity

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