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αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
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αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
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αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine

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αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine
Journal Article

αvβ3 integrin-targeted magnetic resonance imaging in a pancreatic cancer mouse model using RGD-modified liposomes encapsulated with Fe-deferoxamine

2024
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Overview
Magnetic resonance (MR) imaging is a powerful imaging modality for obtaining anatomical information with high spatial and temporal resolution. In the drug delivery system (DDS) framework, nanoparticles such as liposomes are potential candidates for MR imaging. We validated that RGD peptides are possible targeting molecules for pancreatic cancer with α v β 3 integrin expression. This study aimed to evaluate RGD-modified liposomes loaded with ferrioxamine B for pancreatic cancer imaging. We synthesized four types of RGD-modified liposomes encapsulated with ferrioxamine B (SH-, H-, M-, and L-RGD-liposomes). The binding affinity of RGD-modified liposomes was evaluated in a competitive inhibition study using 125 I-echistatin. To investigate the pharmacokinetics of RGD-modified liposomes, a biodistribution study using RGD-liposomes labeled with 111 In was carried out in a human pancreatic cancer PANC-1 xenograft mouse model. Finally, MR was performed using ferrioxamine-B-loaded liposomes. RGD-liposomes inhibited the binding of 125 I-echistatin to RGD. The biodistribution study revealed that 111 In-RGD-liposomes accumulated significantly in the liver and spleen. Among the 111 In-RGD-liposomes, 111 In-H-RGD-liposomes showed the highest tumor-to-normal tissue ratio. In the MR study, H-RGD-liposomes loaded with ferrioxamine B showed higher tumor-to-muscle signal ratios than RKG-liposomes loaded with ferrioxamine B (control). We successfully synthesized RGD-liposomes that can target α v β 3 integrin.