Activated molecular probes for enzyme recognition and detection

Yuan, Meng; Wu, Ying; Zhao, Caiyan; Chen, Zhongxiang; Su, Lichao; Yang, Huanghao; Song, Jibin

doi:10.7150/thno.66676

Cited by 27 publications

(10 citation statements)

References 127 publications

(101 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ease of modification of peptides makes the design of enzyme cleavage‐based sensors more flexible than structure‐based methods and thus has gained more attention in recent years. [ 124 ] In the following section, the use of enzymatic cleavage of peptides in the design of MMPs sensors, including electrochemical, ECL, photoelectrochemical (PEC), fluorescence, chemiluminescence (CL), PA, SERS, mass spectrometry (MS), and magnetic resonance imaging (MRI) sensors are discussed.…”

Section: Enzymatic Activity‐based Sensorsmentioning

confidence: 99%

Recent Development and Applications of Sensors for the Detection of Matrix Metalloproteinases

Zhang

et al. 2023

Adv Materials Technologies

View full text Add to dashboard Cite

of ECM cleavage. As the number of identified MMPs types increased, researchers began to classify the MMPs according to the protein structure. [3] Despite some structural differences, most of the structural modules of MMPs are still conservative, including i) an amino-terminal peptide which can leads MMPs to the endoplasmic reticulum, ii) a propeptide region (companying with a zinc-interacting thiol group) and a zinc-binding site which can maintains MMPs as inactive zymogens or as a catalytic domain, iii) a linker region of varying residue length that may determine the substrates to which the MMPs can accommodate, and iv) a hemopexin-like domain. [4] With the application of engineered genetic models these years, more biological roles of MMPs have been revealed in recently years. For example, through investigating MMPs' substrates of other proteins, such as pro-proteases, chemokines, antimicrobial peptides, cell surface proteins, coagulation factors, adhesion molecules, cryptic growth factors, and cytokines, [5] it has been revealed that the MMPs have a broad and dramatic impact on physiological processes, for example, immunity, [6] tissue repair, [7,8] cell differentiation, [9,10] and cell invasion. [11] In these physiological processes, MMPs are secreted as zymogens. [12] The cysteine (Cys) residues of MMPs' propeptide regions are able to interact with Zn 2+ of the catalytic domains. The formation of the thiols-Zn 2+ bonds play important roles in maintaining the inactivity of MMPs, i.e., MMPs' activations are achieved by breaking these bonds. It is conceivable that MMPs can be activated by a variety of endogenous or exogenous substances, such as mercurial compounds and chaotropic agents. [4] To regulate the activity of MMPs, organisms have evolved a family of two-domain proteins (TIMPs) as the endogenous inhibitors. [13] Most MMPs are ubiquitously secreted in mammalian organisms. The level of MMPs' expression is generally low under normal physiological conditions, while the abnormally elevated expression and activity levels are often associated with diseases. For example, as of the positive roles of MMPs in tumor growth and angiogenesis, [14] recent studies revealed that MMPs overexpression is implicated in a variety of cancers. [15] MMP-2 and MMP-9 are overexpressed in breast cancer, [16] cervical cancer, [17] etc., while MMP-7 are correlated with colorectal cancer (CRC). [18] Moreover, the prognostic value of MMPs has also been well demonstrated in treatment of different cancers. [19,20] For example, patients with high levels of MMP-2 and MMP-9 were clinically defined as a poor prognosis. [21] Therefore, MMPs' Matrix metalloproteinases (MMPs) are a class of zinc-dependent endopeptidases that play important roles in disease progression. High expression of MMPs is associated with various diseases, including cancer, cardiovascular diseases, neurological diseases, and inflammatory diseases. For better understanding the roles of MMPs in these diseases' development and the potential in early diagnosis and treatment m...

show abstract

Section: Enzymatic Activity‐based Sensorsmentioning

confidence: 99%

Recent Development and Applications of Sensors for the Detection of Matrix Metalloproteinases

Zhang

et al. 2023

Adv Materials Technologies

View full text Add to dashboard Cite

show abstract

“…Among these emerging modalities, fluorescence imaging has been the most extensively researched for intraoperative applications due to its advantages of high sensitivity, high visibility, low cost, and high spatial and temporal resolutions. ,, Molecular contrast probes for fluorescence imaging have also been well studied worldwide, and various designs and clinical applications have been reported. , Fluorescence imaging also has the advantage of not requiring expensive equipment. However, it has a significant drawback: imaging deep inside the tissue is difficult owing to the absorption and scattering of excitation (Ex) and emission (Em) light by living tissues.…”

Section: Introductionmentioning

confidence: 99%

“…9,33,34 Molecular contrast probes for fluorescence imaging have also been well studied worldwide, and various designs and clinical applications have been reported. 35,36 Fluorescence imaging also has the advantage of not requiring expensive equipment. However, it has a significant drawback: imaging deep inside the tissue is difficult owing to the absorption and scattering of excitation (Ex) and emission (Em) light by living tissues.…”

mentioning

confidence: 99%

Activity-Based Fluorescence Diagnostics for Cancer

Fujita,

Urano

2024

Chem. Rev.

View full text Add to dashboard Cite

Fluorescence imaging is one of the most promising approaches to achieve intraoperative assessment of the tumor/normal tissue margins during cancer surgery. This is critical to improve the patients' prognosis, and therefore various molecular fluorescence imaging probes have been developed for the identification of cancer lesions during surgery. Among them, "activatable" fluorescence probes that react with cancer-specific biomarker enzymes to generate fluorescence signals have great potential for high-contrast cancer imaging due to their low background fluorescence and high signal amplification by enzymatic turnover. Over the past two decades, activatable fluorescence probes employing various fluorescence control mechanisms have been developed worldwide for this purpose. Furthermore, new biomarker enzymatic activities for specific types of cancers have been identified, enabling visualization of various types of cancers with high sensitivity and specificity. This Review focuses on recent advances in the design, function and characteristics of activatable fluorescence probes that target cancer-specific enzymatic activities for cancer imaging and also discusses future prospects in the field of activity-based diagnostics for cancer. CONTENTS

show abstract

“…This fundamental necessity motivated us to investigate environment‐resistant dyes for fluorescence sensing and bio‐imaging applications [4,6] . The push‐pull type, dipolar fluorophores, such as acedan, coumarin, naphthalimide, Nile blue, and structurally related dyes have been extensively used for developing “activatable” probes by introducing a reactive group to the amino donor: An analyte‐specific chemical transformation at the reactive site produces fluorescence signal change owing to the perturbation in the intramolecular charge transfer [7a,b] . Phenolic fluorophores, hydroxy analogues of those “amino‐fluorophores”, also provide an important dye platform for developing activatable probes.…”

Section: Introductionmentioning

confidence: 99%

A General Strategy Toward pH‐Resistant Phenolic Fluorophores for High‐Fidelity Sensing and Bioimaging Applications

Sarkar,

Shil,

Maity

et al. 2023

Angew Chem Int Ed

View full text Add to dashboard Cite

Aryl alcohol‐type or phenolic fluorophores offer diverse opportunities for developing bioimaging agents and fluorescence probes. Due to the inherently acidic hydroxyl functionality, phenolic fluorophores provide pH‐dependent emission signals. Therefore, except for developing pH probes, the pH‐dependent nature of phenolic fluorophores should be considered in bioimaging applications but has been neglected. Here we show that a simple structural remedy converts conventional phenolic fluorophores into pH‐resistant derivatives, which also offer “medium‐resistant” emission properties. The structural modification involves a single‐step introduction of a hydrogen‐bonding acceptor such as morpholine nearby the phenolic hydroxyl group, which also leads to emission bathochromic shift, increased Stokes shift, enhanced photo‐stability and stronger emission for several dyes. The strategy greatly expands the current fluorophores’ repertoire for reliable bioimaging applications, as demonstrated here with ratiometric imaging of cells and tissues.

show abstract

Activated molecular probes for enzyme recognition and detection

Cited by 27 publications

References 127 publications

Recent Development and Applications of Sensors for the Detection of Matrix Metalloproteinases

Recent Development and Applications of Sensors for the Detection of Matrix Metalloproteinases

Activity-Based Fluorescence Diagnostics for Cancer

A General Strategy Toward pH‐Resistant Phenolic Fluorophores for High‐Fidelity Sensing and Bioimaging Applications

Contact Info

Product

Resources

About