8ZPA
Crystal structure of a HSA/probe complex
Summary for 8ZPA
| Entry DOI | 10.2210/pdb8zpa/pdb |
| Descriptor | Albumin, 7-$l^{3}-oxidanyl-12~{H}-[2,1]benzazaborolo[2,1-a][1,3,2]benzodiazaborinine, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | serum albumin, structural protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 68308.33 |
| Authors | Youn, S.Y.,Cha, S.S. (deposition date: 2024-05-29, release date: 2025-03-05, Last modification date: 2025-03-12) |
| Primary citation | Yang, M.,Kim, Y.,Youn, S.Y.,Jeong, H.,Shirbhate, M.E.,Uhm, C.,Kim, G.,Nam, K.T.,Cha, S.S.,Kim, K.M.,Yoon, J. Conversion of albumin into a BODIPY-like photosensitizer by a flick reaction, tumor accumulation and photodynamic therapy. Biomaterials, 313:122792-122792, 2025 Cited by PubMed Abstract: The accumulation of photosensitizers (PSs) in lesion sites but not in other organs is an important challenge for efficient image guiding in photodynamic therapy. Cancer cells are known to express a significant number of albumin-binding proteins that take up albumin as a nutrient source. Here, we converted albumin to a novel BODIPY-like PS by generating a tetrahedral boron environment via a flick reaction. The formed albumin PS has almost the same 3-dimensional structural feature as free albumin because binding occurs at Sudlow Site 1, which is located in the interior space of albumin. An i.v. injection experiment in tumor-bearing mice demonstrated that the human serum albumin PS effectively accumulated in cancer tissue and, more surprisingly, albumin PS accumulated much more in the cancer tissue than in the liver and kidneys. The albumin PS was effective at killing tumor cells through the generation of reactive oxygen species under light irradiation. The crystal structure of the albumin PS was fully elucidated by X-ray crystallography; thus, further tuning of the structure will lead to novel physicochemical properties of the albumin PS, suggesting its potential in biological and clinical applications. PubMed: 39226652DOI: 10.1016/j.biomaterials.2024.122792 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
Download full validation report
