Loading and release of a model high-molecular-weight protein from temperature-sensitive micro-structured hydrogels
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Research Letter
Loading and release of a model high-molecular-weight protein from temperature-sensitive micro-structured hydrogels Kenia Palomino , Héctor Magaña, Samuel G. Meléndez-López, and José M. Cornejo-Bravo , Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Universidad 14418, Parque industrial Internacional, C.P. 22427 Tijuana B.C., Mexico Aracely Serrano-Medina, Facultad de Medicina y Psicología, Universidad Autónoma de Baja California, Calzada Universidad 14418, Parque industrial Internacional, C.P. 22427 Tijuana B.C., Mexico Manuel Alatorre-Meda, Cátedras CONACyT-Tecnológico Nacional de México/I. T. Tijuana, Centro de Graduados e Investigación en Química-Grupo de Biomateriales y Nanomedicina, Blvd. Alberto Limón Padilla S/N, 22510 Tijuana B.C., Mexico Eustolia Rodríguez-Velázquez, Facultad de Odontología Campus Tijuana, Universidad Autónoma de Baja California, Calzada Universidad 14418, Parque industrial Internacional, 22390 Tijuana B.C., Mexico; Tecnológico Nacional de México/I. T. Tijuana, Centro de Graduados e Investigación en Química − Grupo de Biomateriales y Nanomedicina, Blvd. Alberto Limón Padilla S/N, 22510 Tijuana B.C., Mexico Ignacio Rivero, Tecnológico Nacional de México/I. T. Tijuana, Centro de Graduados e Investigación en Química, Blvd. Alberto Limón Padilla S/N, 22510 Tijuana B.C., Mexico Address all correspondence to J.M. Cornejo-Bravo at [email protected] (Received 2 May 2019; accepted 17 June 2019)
Abstract The authors prepared a micro-structured, thermosensitive hydrogel with N-isopropylacrylamide microgels with a lower critical solution temperature (LCST) of 32 °C dispersed on a matrix of N-isopropylacrylamide-co-dimethylacrylamide with an LCST at 40 °C. Incubation of the hydrogel at 33 °C in a solution of fluorescein-albumin induced loading of the protein. The protein was not loaded at a temperature below the LCST of the microgels (4 °C), suggesting that the shrinkage of the microgels followed by the formation of micropores within the hydrogel matrix is a prerequisite for protein loading. A sustained and complete release of the loaded protein was obtained at 37 °C.
Introduction Proteins have become important therapeutic agents for the treatment of diverse pathologies.[1] However, most therapeutic proteins lack stability because of the high risk for proteolytic and chemical degradation, as well as denaturation and aggregation. This has resulted in an increased demand for materials that are able to protect proteins from hostile environments and to control their release.[2–8] N-isopropylacrylamide (NIPAAm) hydrogels present a swollen-to-unswollen transition at an LCST of 32 °C.[9] NIPAAm hydrogels have been studied for the loading and release of insulin (5.8 kDa) and albumin (66.5 kDa). Such studies demonstrated the complete release of insulin; nevertheless, physical entanglement precluded the complete release of albumin from the hydrogels, either at a constant temperature or with oscillating swelling–deswelling in response to temperature
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