H
Hongkee Sah
Researcher at Ewha Womans University
Publications - 72
Citations - 2545
Hongkee Sah is an academic researcher from Ewha Womans University. The author has contributed to research in topics: PLGA & Aqueous solution. The author has an hindex of 19, co-authored 71 publications receiving 2357 citations. Previous affiliations of Hongkee Sah include Temple University & Catholic University of Daegu.
Papers
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Journal ArticleDOI
Core–shell-type lipid–polymer hybrid nanoparticles as a drug delivery platform
Bivash Mandal,Himanshu Bhattacharjee,Nivesh K. Mittal,Hongkee Sah,Pavan Balabathula,Laura A. Thoma,George C. Wood +6 more
TL;DR: This comprehensive review covers the current applications of core-shell-type lipid-polymer hybrid nanoparticles, which combine the mechanical advantages of biodegradable polymeric nanoparticles and biomimetic advantages of liposomes to enable an efficient drug delivery system.
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Stabilization of proteins against methylene chloride/water interface-induced denaturation and aggregation.
TL;DR: This study substantiated that an adequate formulation could overcome denaturing effects of the methylene chloride/water interface upon a protein of interest to be encapsulated into microspheres.
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Concepts and practices used to develop functional PLGA-based nanoparticulate systems
TL;DR: Fundamental concepts and practices used in the development of various functional nanoparticulate dosage forms are described to contribute to achievement of desired therapeutic effects that are not attainable using conventional therapies.
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Microencapsulation techniques using ethyl acetate as a dispersed solvent: Effects of its extraction rate on the characteristics of PLGA microspheres
TL;DR: In this article, the effects of the O:W1 phase ratio on the morphology and size of microspheres were interpreted in terms of the solvent miscibility with water, as well as the influence of the W1 volume on breakup of the dispersed phase.
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Protein behavior at the water/methylene chloride interface
TL;DR: Results indicated that competitive adsorption modes of proteins could be used to stabilize a protein of interest against the denaturing effects of emulsification.