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Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407

The combination of the thermoresponsive polymer and protein has demonstrated great promise in its applications in drug delivery and tissue engineering fields. This study described the impact of bovine serum albumin (BSA) on the micellization and sol–gel transition behaviors of poloxamer 407 (PX). Th...

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Autores principales: Hirun, Namon, Kraisit, Pakorn, Soontaranon, Siriwat
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10255380/
https://www.ncbi.nlm.nih.gov/pubmed/37299264
http://dx.doi.org/10.3390/polym15112465
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author Hirun, Namon
Kraisit, Pakorn
Soontaranon, Siriwat
author_facet Hirun, Namon
Kraisit, Pakorn
Soontaranon, Siriwat
author_sort Hirun, Namon
collection PubMed
description The combination of the thermoresponsive polymer and protein has demonstrated great promise in its applications in drug delivery and tissue engineering fields. This study described the impact of bovine serum albumin (BSA) on the micellization and sol–gel transition behaviors of poloxamer 407 (PX). The micellization of aqueous PX solutions with and without BSA was examined using isothermal titration calorimetry. In the calorimetric titration curves, the pre-micellar region, the transition concentration region, and the post-micellar region were observed. The presence of BSA had no noticeable impact on critical micellization concentration, but the inclusion of BSA caused the pre-micellar region to expand. In addition to studying the self-organization of PX at a particular temperature, the temperature-induced micellization and gelation of PX were also explored using differential scanning calorimetry and rheology. The incorporation of BSA had no discernible effect on critical micellization temperature (CMT), but it did affect gelation temperature (T(gel)) and gel integrity of PX-based systems. The response surface approach illustrated the linear relation between the compositions and the CMT. The major factor affecting the CMT of the mixtures was the concentration of PX. The alteration of the T(gel) and the gel integrity were discovered to be a consequence of the intricate interaction between PX and BSA. BSA mitigated the inter-micellar entanglements. Hence, the addition of BSA demonstrated a modulating influence on T(gel) and a softening effect on gel integrity. Understanding the influence of serum albumin on the self-assembly and gelation of PX will enable the creation of thermoresponsive drug delivery and tissue engineering systems with controlled gelation temperatures and gel strength.
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spelling pubmed-102553802023-06-10 Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407 Hirun, Namon Kraisit, Pakorn Soontaranon, Siriwat Polymers (Basel) Article The combination of the thermoresponsive polymer and protein has demonstrated great promise in its applications in drug delivery and tissue engineering fields. This study described the impact of bovine serum albumin (BSA) on the micellization and sol–gel transition behaviors of poloxamer 407 (PX). The micellization of aqueous PX solutions with and without BSA was examined using isothermal titration calorimetry. In the calorimetric titration curves, the pre-micellar region, the transition concentration region, and the post-micellar region were observed. The presence of BSA had no noticeable impact on critical micellization concentration, but the inclusion of BSA caused the pre-micellar region to expand. In addition to studying the self-organization of PX at a particular temperature, the temperature-induced micellization and gelation of PX were also explored using differential scanning calorimetry and rheology. The incorporation of BSA had no discernible effect on critical micellization temperature (CMT), but it did affect gelation temperature (T(gel)) and gel integrity of PX-based systems. The response surface approach illustrated the linear relation between the compositions and the CMT. The major factor affecting the CMT of the mixtures was the concentration of PX. The alteration of the T(gel) and the gel integrity were discovered to be a consequence of the intricate interaction between PX and BSA. BSA mitigated the inter-micellar entanglements. Hence, the addition of BSA demonstrated a modulating influence on T(gel) and a softening effect on gel integrity. Understanding the influence of serum albumin on the self-assembly and gelation of PX will enable the creation of thermoresponsive drug delivery and tissue engineering systems with controlled gelation temperatures and gel strength. MDPI 2023-05-26 /pmc/articles/PMC10255380/ /pubmed/37299264 http://dx.doi.org/10.3390/polym15112465 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Hirun, Namon
Kraisit, Pakorn
Soontaranon, Siriwat
Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title_full Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title_fullStr Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title_full_unstemmed Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title_short Role of Bovine Serum Albumin Addition in Micellization and Gel Formation of Poloxamer 407
title_sort role of bovine serum albumin addition in micellization and gel formation of poloxamer 407
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10255380/
https://www.ncbi.nlm.nih.gov/pubmed/37299264
http://dx.doi.org/10.3390/polym15112465
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