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Background: The accurate and rapid detection of blood lead concentration is of paramount importance for assessing human lead exposure levels. Fluorescent protein-based probes, known for their high detection capabilities and low toxicity, are extensively used in analytical sciences. However, there is currently a shortage of such probes designed for ultrasensitive detection of Pb, and no reported probes exist for the quantitative detection of Pb in blood samples. This study aims to fill this critical void by developing and evaluating a novel fluorescent protein-based probe that promises accurate and rapid lead quantification in blood.
Results: A simple and small-molecule fluorescent protein-based probe was successfully constructed herein using a peptide PbrBD designed for Pb recognition coupled to a single fluorescent protein, sfGFP. The probe retains a three-coordinate configuration to identify Pb and has a high affinity for it with a K' of 1.48 ± 0.05 × 10 M. It effectively transfers the conformational changes of the peptide to the chromophore upon Pb binding, leading to fast fluorescence quenching and a sensitive response to Pb. The probe offers a broad dynamic response range of approximately 37-fold and a linear detection range from 0.25 nM to 3500 nM. More importantly, the probe can resist interference of metal ions in living organisms, enabling quantitative analysis of Pb in the picomolar to millimolar range in serum samples with a recovery percentage of 96.64%-108.74 %.
Significance: This innovative probe, the first to employ a single fluorescent protein-based probe for ultrasensitive and precise analysis of Pb in animal and human serum, heralds a significant advancement in environmental monitoring and public health surveillance. Furthermore, as a genetically encoded fluorescent probe, this probe also holds potential for the in vivo localization and concentration monitoring of Pb.
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http://dx.doi.org/10.1016/j.aca.2024.342580 | DOI Listing |
ACS Sens
September 2025
Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Kowloon 999077, Hong Kong SAR China.
The persistence of plastics in the environment, especially after waste disposal, poses a significant threat to ecosystems. Microplastics (MPs) are particularly concerning due to their small size and the difficulty of detection. Once in aquatic systems, MPs threaten marine life and human health through the food chain.
View Article and Find Full Text PDFJ Med Chem
September 2025
Department of Chemistry, University of Toronto, 3359 Mississauga Road, Mississauga, Ontario L5L 1C6, Canada.
Overexpression of the proto-oncogene MYC occurs in >70% of cancers and is especially prevalent in breast cancer. Myc partners with transcription factor Max to bind to the E-box DNA response element. By patterning our frankenproteins on the basic region/helix-loop-helix/leucine zipper motif of Max, we designed MEF and MEF/C93 to bind to the E-box.
View Article and Find Full Text PDFAdv Funct Mater
January 2025
Department of Bioengineering, University of California, Los Angeles, CA 90095, USA.
Cell reprogramming and manufacturing have broad applications in tissue regeneration and disease treatment. However, many derived cell types lack unique cell surface markers for protein-based cell sorting, making it difficult to isolate these cells from mixed populations. Additionally, there is a need to identify and isolate cells of interest at the early stages of cell expansion.
View Article and Find Full Text PDFFoods
August 2025
College of Grain Science and Technology, Shenyang Normal University, Shenyang 110034, China.
Meat analog manufacturing via high-moisture extrusion technology is a complex process wherein the properties of protein materials constitute a critical determining factor. In this study, we enhanced the fiber structure properties of high-moisture extruded peanut protein-based meat analogs by incorporating different starches (cassava starch, acetyl distarch phosphate [ADSP], and hydroxypropyl starch) to address challenges in water retention, emulsification, and digestibility. The impact of the starch content (0, 3, 6, 9, 12%) was assessed using low-field nuclear magnetic resonance, ultraviolet/fluorescence spectroscopy, differential scanning calorimetry, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and functional tests.
View Article and Find Full Text PDFSheng Wu Gong Cheng Xue Bao
August 2025
School of Biomedical Sciences and Engineering, South China University of Technology, Guangzhou 510006, Guangdong, China.
In this study, we constructed a series of recombinant Fc variants of immunoglobulin G4 (IgG4), screened the fragment crystallizable (Fc) variants with significantly prolonged serum half-lives, and analyzed the relationship between mutation site and half-life, aiming to provide a theoretical basis for the development of IgG4 antibodies and Fc fusion protein-based drugs. Nine gene sites were selected for mutation, and different mutation sites were combined. The variant expression plasmids pET24b-Fc were constructed by molecular cloning and point mutation.
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