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Innovative design of CXCR4 cyclic peptide via molecular docking for 99mTc-Labeled SPECT/CT imaging in melanoma
Xianrui Yin1, Xin Wang2, Chengwei Chen3
1Department of Nuclear Medicine, Mianyang Central Hospital, School of Medicine, University of Electronic Science and Technology of China, Mianyang, China; Mianyang Key Laboratory of Anesthesia and Neuroregulation, Department of Anesthesiology, Mianyang Central Hospital, Mianyang, 621000, China; NHC Key Laboratory of Nuclear Technology Medical Transformation, Mianyang Central Hospital, Mianyang, China; Department of Nuclear Medicine, The First Affiliated Hospital of Air Force Medical University, Xi'an, Shaanxi, 710032, China.
Backgroud:
The chemokine receptor CXCR4 is a crucial target for the diagnosis and treatment of cancer due to its close association with tumor growth, metastasis, invasiveness, and prognosis.
Results:
The cyclic peptides KC1 and KC1E, along with their radiolabeled conjugates [99mTc]Tc-HYNIC-KC1 and [99mTc]Tc-HYNIC-KC1E, were successfully synthesized. The binding affinity of KC1 toward the CXCR4 receptor was evaluated using Surface Plasmon Resonance (SPR). Furthermore, key physicochemical and biological properties of the radiotracers were systematically assessed, including the oil-water partition coefficient (LogP), in vitro stability in normal saline solution and mouse serum, in vivo SPECT/CT imaging performance in a B16-F10 tumor-bearing mouse model, and biodistribution profiles following intravenous administration.
Significance:
A novel cyclic peptide, KC1, was designed and shown to exhibit selective binding to the CXCR4 receptor. Molecular docking simulations were performed to elucidate the potential interaction mechanism between KC1 and CXCR4. The radiolabeled derivative [99mTc]Tc-HYNIC-KC1E was synthesized and demonstrated favorable in vivo imaging performance in B16-F10 tumor-bearing mice, supporting its potential as a promising imaging agent for CXCR4-positive tumors.
Insights
Researchers developed a novel cyclic peptide, KC1, that selectively binds to the CXCR4 receptor. Its radiolabeled form, [99mTc]Tc-HYNIC-KC1E, shows promise as an imaging agent for CXCR4-positive tumors.
Area of Science:
- Oncology
- Radiochemistry
- Molecular Imaging
Background:
- Chemokine receptor CXCR4 is a key target in cancer diagnosis and treatment.
- CXCR4 expression correlates with tumor growth, metastasis, invasiveness, and patient prognosis.
Purpose of the Study:
- To design and synthesize a novel cyclic peptide targeting CXCR4.
- To evaluate the binding affinity and imaging potential of the peptide and its radiolabeled derivative.
Main Methods:
- Synthesis of cyclic peptides KC1 and KC1E and their radiolabeled conjugates.
- Surface Plasmon Resonance (SPR) for binding affinity assessment.
- Evaluation of physicochemical properties (LogP, stability) and in vivo SPECT/CT imaging in a B16-F10 tumor model.
Main Results:
- Successful synthesis of KC1, KC1E, [99mTc]Tc-HYNIC-KC1, and [99mTc]Tc-HYNIC-KC1E.
- KC1 demonstrated selective binding to CXCR4.
- The radiotracer [99mTc]Tc-HYNIC-KC1E exhibited favorable in vivo SPECT/CT imaging performance in tumor-bearing mice.
Conclusions:
- A novel cyclic peptide, KC1, selectively binds to CXCR4.
- The radiolabeled derivative [99mTc]Tc-HYNIC-KC1E is a promising imaging agent for CXCR4-positive tumors.
- Molecular docking elucidated the interaction mechanism between KC1 and CXCR4.
