Peptide Modification for Scientific Research Tool

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With the continuous progress of science and technology, peptide modification technology plays an increasingly important role in the development of scientific research tools. Through various chemical modifications, peptides are not only suitable for technologies such as mass spectrometry and nuclear magnetic resonance, but also help to promote the development of life science research. As a key tool in bioscience research, peptides have shown a wide range of application potential after modification. In this article, we will delve into several important application areas of peptide modification technology in the development of scientific research tools, and demonstrate its key role in life science research through specific cases.

Modify the biosensor with peptides

The application of peptides on the surface of biosensors can significantly improve the selectivity and sensitivity of specific biomolecule detection. As one of the major threats to global public health, rapid and accurate detection of Staphylococcus aureus is particularly crucial. The research team from Jiangnan University successfully screened two peptide molecules that can efficiently bind to Staphylococcus aureus through phage display technology, named PEP23 and PEP28, respectively. Subsequently, they modified these peptide molecules and used these modified peptide molecules to construct gold nanoparticle biosensors. This biosensor excels in point-of-care detection of Staphylococcus aureus, with a sensitivity of up to 2.35 CFU per milliliter and the detection process completed in as little as 90 minutes. This technological breakthrough shows that through careful selection of appropriate peptide sequences and effective modification strategies, the sensor can demonstrate extremely high recognition and responsiveness to the target molecule. This not only provides a powerful tool for detection and diagnosis, but also provides a substantial solution to the health threat posed by pathogens such as Staphylococcus aureus. With the further optimization and expansion of the technology, this peptide molecule-based modification biosensor is expected to play a wider role in clinical practice. This includes, but is not limited to, the detection of other pathogenic bacteria and the quantitative analysis of biomolecules, so as to promote the precision of early diagnosis and treatment and provide a solid guarantee for public health and safety.

Fig.1 Construction of the colorimetric immunosensor based on the two PDPs for S. aureus. (Wu Shang, et al., 2024)

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Contrast modifying peptides on magnetic resonance imaging

Magnetic resonance imaging (MRI) has become an important tool in experimental and clinical radiology due to its deep tissue penetration, excellent soft tissue contrast, and spatiotemporal resolution without ionizing radiation. Luo and his research group have developed an innovative MRI probe, the Enzyme-Responsive Peptide MR Probe (TSP) based on chlorophyll derivatives. The design of the probe includes a peptide sequence targeting a region-targeted mannose fragment, a peptide sequence with a cathepsin B enzyme cleavage site, and a chlorophyll derivative fragment of the paramagnetic contrast agent Mn₂⁺. This probe has multiple functions: first, it is able to actively target the CD206 receptor, which is an important marker on the surface of macrophages. Upon entry into CD206-overexpressing macrophages, the probe undergoes in situ assembly, specifically interacting with cathepsin B. This molecular-level interaction not only effectively enhances the MRI T1 signal, but also significantly extends the detection time window, improving the sensitivity and resolution of imaging.

Due to its targeting and enzyme response properties, this peptide molecular probe is not only important in laboratory research, but also shows potential to be a safe and effective MRI enhancer. In the future, with the further optimization and application expansion of such technologies, it is expected to bring more breakthroughs in clinical practice, providing more accurate molecular-level information for disease diagnosis and treatment.

Fig.2 Schematic diagram of the MR probe TSP design. (Luo Lu-Jun, et al., 2022)

Isotopically modified heavy peptides in Instrumental Analysis

Isotopically labeled heavy peptides play an important role in scientific research, especially in the fields of mass spectrometry (MS) and nuclear magnetic resonance (NMR). These heavy peptides form known molecular weight differences by replacing the standard ¹²C and ¹⁴N atoms with ¹³C and/or ¹⁵N isotopes. This labeling technique enables heavy peptides to play a key role in quantitative peptide analysis and studying protein structural dynamics, significantly improving the accuracy and confidence of the data. For example, heavy peptide labeling techniques can be used to precisely determine the quantitative changes of proteins under different conditions, while exploring the structure and function of proteins at the molecular level. These technological advances have not only advanced the understanding of biomolecules, but also provided important experimental tools for drug design and disease research.

Biotinylated peptides in immunoassays

Biotinylated peptides are techniques for covalently attaching biotin (biotin) to the N-terminus or lysine (Lys) side chain of a peptide. Due to the strong affinity between biotin-streptavidin and avidin, biotin-labeled peptides are widely used in immunoassays, histochemistry, and fluorescence-based flow cytometry. Labeled anti-biotin antibodies can be used to specifically bind biotinylated peptides. Biotin is usually attached to the lysine side chain or N-terminus, and this label can be precisely controlled at a specific location in the peptide by chemical synthesis. In order to establish a stable link between the peptide and biotin, 6-aminocaproic acid is often used as a link. This bond is flexible enough to accommodate a wide range of structural and steric obstruction situations, ensuring that biotin binds to it more strongly and effectively. These labeled peptides can bind to streptavidin, for example, to form stable complexes, allowing researchers to efficiently detect and analyze the expression and distribution of target proteins or cellular molecules.

Summary

Peptide modification technology not only improves the application efficiency and accuracy of scientific research tools in life science research, but also brings new opportunities and breakthroughs to the development of mass spectrometry, immunoassays, and biosensors. With the continuous innovation and application of technology, it is expected that peptide modification will continue to play an important role in scientific research and biomedical fields, providing innovative solutions to solve complex biological problems.

References

1. Wu, Shang, et al., Double phage displayed peptides co-targeting-based biosensor with signal enhancement activity for colorimetric detection of Staphylococcus aureus. Biosensors and Bioelectronics 249 (2024): 116005.
2. Luo, Lu-Jun, et al., Quantitative detection of in vivo aggregation degree for enhanced M2 macrophage MR imaging. Nano Letters 22.4 (2022): 1694-1702.