윤소연 (이화여자대학교, 토드제약)

한빛사논문

조회162

이화여자대학교, 토드제약

Biomaterials, Aug 30 2024, 313 S0142-9612(24)00326-0 | https://doi.org/10.1016/j.biomaterials.2024.122792 Conversion of albumin into a BODIPY-like photosensitizer by a flick reaction, tumor accumulation and photodynamic therapy

Mengyao Yang ^a,1, Yujin Kim ^a,1, So-Yeon Youn ^a,d,1, Haengdueng Jeong^b,1, Mukesh Eknath Shirbhate^c, Chanyang Uhm ^b, Gyoungmi Kim^c, Ki Taek Nam ^b, Sun-Shin Cha^a,d, Kwan Mook Kim ^a, Juyoung Yoon ^a

^aDepartment of Chemistry and Nanoscience, Ewha Womans University, Seoul, 03760, South Korea

^bDepartment of Biomedical Sciences, Brain Korea 21 PLUS Project for Medical Science, College of Medicine, Yonsei University, Seoul, 03760, South Korea

^cResearch Center for Biomaterials, KYTECBIO, Ewhayeodae-gil 52, Seoul, 03760, South Korea

^dTODD PHARM, Ewha Womans University, Seoul, 03760, South Korea

¹These authors contributed equally to this work.

Corresponding authors: Ki Taek Nam, Sun-Shin Cha, Kwan Mook Kim, Juyoung Yoon

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.

논문정보

형식Research article
게재일2024년 08월 (BRIC 등록일 2024-09-05)
연구진국내 연구진
분야 바이오·의료융합 > 바이오소재

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