Visualized characterization of bacterial penicillin G acylase for the hydrolysis of β-lactams using an activatable NIR fluorescent probe

Tian, Zhenhao; Feng, Lei; Li, Lü; Tian, Xiangge; Cui, Jingnan; Zhang, Hou-Li; Wang, Chao; Huang, Huilian; Zhang, Baojing; Ma, Xiaochi

doi:10.1016/j.snb.2020.127872

Cited by 12 publications

(3 citation statements)

References 30 publications

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“…Penicillin G acylase (PGA), derived from microorganisms like bacteria, fungi, yeast, and actinomycetes, is a unique and important enzyme in industrial settings. Its primary function involves catalyzing the enzymatic hydrolysis of various penicillins by breaking the amide side chain, thereby producing 6-aminopenicillanic acid (6-APA) (Tian et al, 2020). Penicillin G is a substrate that is enzymatically converted for the synthesis of new β-lactam antibiotics such as amoxicillin .…”

Section: Introductionmentioning

confidence: 99%

Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

Amin,

Sismindari,

Aniqah

et al. 2024

Indonesian J Pharm

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The strategy of producing PGA on a massive scale with high levels of soluble protein can be through recombinant genetic techniques and expressed in a certain host. E. coli is still a popular bacterial host to produce a recombinant protein which has advantages such as fast growth, low production cost, and high expression rate. Apart from its advantages, E. coli as a production host also has disadvantages including the expression of recombinant proteins often failing to form the proper folding conformation which makes the protein biologically inactive. Many strategies can be developed to overcome these problems, such as the selection of the host strain (E. coli HB101 & JM109), fusion protein to enhance the recovery of soluble protein (MBP & NusA), optimization of fermentation (low-temperature incubation), and optimization of the protein isolation process for the recovery of active PGA (Freeze-thawing method).

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Section: Introductionmentioning

confidence: 99%

Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

Amin,

Sismindari,

Aniqah

et al. 2024

Indonesian J Pharm

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“…As is known, fluorescent probe with near-infrared (NIR) emission is widely regarded as an ideal candidate for bioimaging in living system due to its superiorities of deep tissue penetration and minimum background autofluorescence 30 , 31 , 32 , 33 , 34 , 35 . Herein, based on the catalytic characteristics of Vanin-1, a novel NIR fluorescent probe DDAV was designed and developed by conjugating pantothenic acid with the NIR fluorophore DDAN.…”

Section: Introductionmentioning

confidence: 99%

A NIR fluorescent probe for Vanin-1 and its applications in imaging, kidney injury diagnosis, and the development of inhibitor

Tian

Yan

Tian

et al. 2022

Acta Pharmaceutica Sinica B

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Vanin-1 is an amidohydrolase that catalyses the conversion of pantetheine into the amino-thiol cysteamine and pantothenic acid (coenzyme A precursor), which plays a vital role in multiple physiological and pathological processes. In this study, an enzyme-activated near-infrared (NIR) fluorescent probe (DDAV) has been constructed for sensitively detecting Vanin-1 activity in complicated biosamples on the basis of its catalytic characteristics. DDAV exhibited a high selectivity and sensitivity toward Vanin-1 and was successfully applied to the early diagnosis of kidney injury in cisplatin-induced kidney injury model. In addition, DDAV could serve as a visual tool for in situ imaging endogenous Vanin-1 in vivo . More importantly, Enterococcus faecalis 20247 which possessed high expression of Vanin-1 was screened out from intestinal bacteria using DDAV, provided useful guidance for the rational use of NSAIDs in clinic. Finally, oleuropein as a potent natural inhibitor for Vanin-1 was discovered from herbal medicines library using a high-throughput screening method using DDAV, which held great promise for clinical therapy of inflammatory bowel disease.

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“…The LOD achieved by the thiol-releasing probe 3 compares to reported fluorescent probes. For example, Tian et al 11 developed a DDAP NIR probe which showed a fluorescence detection of PGA between 0.001-0.004 U mL À1 PGA. While fluorogenic probes are indeed able to detect low concentrations of enzymes via a 1 : 1 enzyme to fluorescent probe ratio, by using DETECT we are able to detect 0.00014 U mL À1 PGA (160 nM) via absorption spectroscopy.…”

mentioning

confidence: 99%

A self-immolative linker that releases thiols detects penicillin amidase and nitroreductase with high sensitivity via absorption spectroscopy

Espinoza

Røise

et al. 2022

Chem. Commun.

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Visualized characterization of bacterial penicillin G acylase for the hydrolysis of β-lactams using an activatable NIR fluorescent probe

Cited by 12 publications

References 30 publications

Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

Manipulation Strategy to Increase Expression Level of Soluble Recombinant Protein Penicillin G Acylase (PGA) in Bacterial Host Escherichia coli: A Review Article

A NIR fluorescent probe for Vanin-1 and its applications in imaging, kidney injury diagnosis, and the development of inhibitor

A self-immolative linker that releases thiols detects penicillin amidase and nitroreductase with high sensitivity via absorption spectroscopy

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