A near-infrared fluorescent probe for monitoring leucine aminopeptidase in living cells

Chai, Yun; Gao, Yuting; Xiong, Huiwen; Lv, Wanqian; Yang, Guichun; Lu, Cuifen; Nie, Junqi; Ma, Chao; Chen, Zuxing; Ren, Jing; Wang, Feiyi

doi:10.1039/c8an01486h

Cited by 25 publications

(26 citation statements)

References 37 publications

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“…LAPs are a class of metal peptidases that hydrolyze leucine residues at the amino terminus of a protein or peptide substrate 59 . LAPs are involved in various physiological processes, including hydrolysis of biologically active peptides 98 , degradation of DNA 99 , and interaction with peptide-dependent signals 100 . LAPs play a vital role in normal functioning of the body 56 .…”

Section: Peptide/group Selective To Enzymesmentioning

confidence: 99%

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Activated molecular probes for enzyme recognition and detection

Yuan¹,

Wu²,

Zhao³

et al. 2022

Theranostics

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Exploring and understanding the interaction of changes in the activities of various enzymes, such as proteases, phosphatases, and oxidoreductases with tumor invasion, proliferation, and metastasis is of great significance for early cancer diagnosis. To detect the activity of tumor-related enzymes, various molecular probes have been developed with different imaging methods, including optical imaging, photoacoustic imaging (PAI), magnetic resonance imaging, positron emission tomography, and so on. In this review, we first describe the biological functions of various enzymes and the selectively recognized chemical linkers or groups. Subsequently, we systematically summarize the design mechanism of imaging probes and different imaging methods. Finally, we explore the challenges and development prospects in the field of enzyme activity detection. This comprehensive review will provide more insight into the design and development of enzyme activated molecular probes.

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Section: Peptide/group Selective To Enzymesmentioning

confidence: 99%

“…Abnormal expression or altered activity of LAPs can lead to tumor invasion 101 . In fact, overexpression of LAPs has been observed in various human diseases, including hepatocellular carcinoma, breast cancer, and endometrial cancer 99 , thereby indicating that LAPs are a potential tumor predictive marker 102 .…”

Section: Peptide/group Selective To Enzymesmentioning

confidence: 99%

Activated molecular probes for enzyme recognition and detection

Yuan¹,

Wu²,

Zhao³

et al. 2022

Theranostics

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“…This probe triggers the L-leucine moiety and can be used to investigate LAP activity in different types of cells [ 39 ]. Later, a new class of probes containing an NIR-fluorophore, CHMC-M-Leu, was developed to monitor endogenous LAP activity in living cells [ 40 ]. Prolyl aminopeptidase (PAP) is an exopeptidase that can be used as a biomarker in pathogenic infections and several cancers.…”

Section: Hydrolase Activity Probementioning

confidence: 99%

Chemical Probes and Activity-Based Protein Profiling for Cancer Research

Mazid

Park

Cheekatla

et al. 2022

IJMS

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Chemical probes can be used to understand the complex biological nature of diseases. Due to the diversity of cancer types and dynamic regulatory pathways involved in the disease, there is a need to identify signaling pathways and associated proteins or enzymes that are traceable or detectable in tests for cancer diagnosis and treatment. Currently, fluorogenic chemical probes are widely used to detect cancer-associated proteins and their binding partners. These probes are also applicable in photodynamic therapy to determine drug efficacy and monitor regulating factors. In this review, we discuss the synthesis of chemical probes for different cancer types from 2016 to the present time and their application in monitoring the activity of transferases, hydrolases, deacetylases, oxidoreductases, and immune cells. Moreover, we elaborate on their potential roles in photodynamic therapy.

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“…To overcome the water insolubility issues of some NIR fluorophores, Wang et al developed a more water-soluble LAP probe (CHMC-M-Leu) by introducing a morpholine moiety on the fluorescent reporter and to improve reactivity a p -aminobenzyl alcohol (PABA) as a self-immolative linker between the fluorophore and leucine ( Figure 2 ). 36 Upon the addition of LAP, great enhancement of fluorescence was observed at 625 nm due to substrate cleavage, and this probe was successfully employed to visualize LAP activity in HeLa cells.…”

Section: Introductionmentioning

confidence: 99%

Near-Infrared Fluorescent Probes for the Detection of Cancer-Associated Proteases

2021

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Proteases are enzymes capable of catalyzing protein breakdown, which is critical across many biological processes. There are several families of proteases, each of which perform key functions through the degradation of specific proteins. As our understanding of cancer improves, it has been demonstrated that several proteases can be overactivated during the progression of cancer and contribute to malignancy. Optical imaging systems that employ near-infrared (NIR) fluorescent probes to detect protease activity offer clinical promise, both for early detection of cancer as well as for the assessment of personalized therapy. In this Review, we review the design of NIR probes and their successful application for the detection of different cancer-associated proteases.

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A near-infrared fluorescent probe for monitoring leucine aminopeptidase in living cells

Abstract: A novel water-soluble near-infrared fluorescent probe (CHMC-M-Leu) for specific monitoring of LAP in vitro and in vivo.

Cited by 25 publications

References 37 publications

Activated molecular probes for enzyme recognition and detection

Activated molecular probes for enzyme recognition and detection

Chemical Probes and Activity-Based Protein Profiling for Cancer Research

Near-Infrared Fluorescent Probes for the Detection of Cancer-Associated Proteases

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