한빛사논문
UNIST
Boram Son1†, Minju Kim2†, Hyosub Won1†, Ara Jung3,4, Jihyun Kim1, Yonghoe Koo2, Na Kyeong Lee5, Seung-Ho Baek6, Uiyoung Han7, Chun Gwon Park8, Heungsoo Shin1, Bomi Gweon3*, Jinmyoung Joo2,9,10* and Hee Ho Park1,11*
1Department of Bioengineering, Hanyang University, Seoul, Republic of Korea
2Department of Biomedical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, Republic of Korea
3Department of Mechanical Engineering, Sejong University, Seoul, Republic of Korea
4Department of Biomedicine & Health Science, College of Medicine, The Catholic University of Korea, Seoul, Korea
5Department of Intelligent Precision Healthcare Convergence, Sungkyunkwan University (SKKU), Suwon, Republic of Korea
6Center for Bio-based Chemistry, Korea Research Institute of Chemical Technology (KRICT), Ulsan, Korea
7Department of Ophthalmology, Stanford University School of Medicine, Stanford, CA, USA
8Department of Biomedical Engineering, SKKU Institute for Convergence, Sungkyunkwan University (SKKU), Suwon, Republic of Korea
9Materials Research Science and Engineering Center, University of California, San Diego, La Jolla, United States
10Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan, Republic of Korea
11Research Institute for Convergence of Basic Science, Hanyang University, Seoul, Republic of Korea
Boram Son, Minju Kim and Hyosub Won contributed equally to this work.
Corresponding authors : Correspondence to Bomi Gweon, Jinmyoung Joo or Hee Ho Park.
Abstract
Background: Basic fibroblast growth factor (bFGF) is one of the critical components accelerating angiogenesis and tissue regeneration by promoting the migration of dermal fibroblasts and endothelial cells associated with matrix formation and remodeling in wound healing process. However, clinical applications of bFGF are substantially limited by its unstable nature due to rapid decomposition under physiological microenvironment.
Results: In this study, we present the bFGF-loaded human serum albumin nanoparticles (HSA-bFGF NPs) as a means of enhanced stability and sustained release platform during tissue regeneration. Spherical shape of the HSA-bFGF NPs with uniform size distribution (polydispersity index < 0.2) is obtained via a simple desolvation and crosslinking process. The HSA-bFGF NPs securely load and release the intact soluble bFGF proteins, thereby significantly enhancing the proliferation and migration activity of human dermal fibroblasts. Myofibroblast-related genes and proteins were also significantly down-regulated, indicating decrease in risk of scar formation. Furthermore, wound healing is accelerated while achieving a highly organized extracellular matrix and enhanced angiogenesis in vivo.
Conclusion: Consequently, the HSA-bFGF NPs are suggested not only as a delivery vehicle but also as a protein stabilizer for effective wound healing and tissue regeneration.
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