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Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release
Protein–peptide–calcium phosphate composites were developed for achieving sustainable and controlled protein release. Bovine serum albumin (BSA) as a model acidic protein was efficiently encapsulated with basic polypeptides such as polylysine and polyarginine during the precipitation of calcium phos...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7287863/ https://www.ncbi.nlm.nih.gov/pubmed/32423135 http://dx.doi.org/10.3390/molecules25102312 |
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author | Kato, Katsuya Lee, Sungho Nagata, Fukue |
author_facet | Kato, Katsuya Lee, Sungho Nagata, Fukue |
author_sort | Kato, Katsuya |
collection | PubMed |
description | Protein–peptide–calcium phosphate composites were developed for achieving sustainable and controlled protein release. Bovine serum albumin (BSA) as a model acidic protein was efficiently encapsulated with basic polypeptides such as polylysine and polyarginine during the precipitation of calcium phosphate (CaP). The prepared composites were fully characterized in terms of their morphologies, crystallinities, and the porosity of their structures, and from these analyses, it was observed that there are no significant differences between the composites. Scanning transmission electron microscopy and energy dispersive X-ray spectroscopy analysis indicated a homogeneous distribution of nitrogen and sulfur, confirming the uniform distribution of BSA and polypeptide in the CaP composite. In vitro release studies demonstrated that the composite prepared with the peptides α-polylysine and polyarginine were suitable for the gradual release of the protein BSA, while those containing ε-polylysine and no peptide were unsuitable for protein release. Additionally, these composites showed high hemocompatibility for mouse red blood cells, and the osteoblast-like cell proliferation and spread in media with the composites prepared using BSA and α-polylysine showed similar tendencies to medium with no composite. From these results, protein–peptide–CaP composites are expected to be useful as highly biocompatible protein delivery agents. |
format | Online Article Text |
id | pubmed-7287863 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-72878632020-06-15 Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release Kato, Katsuya Lee, Sungho Nagata, Fukue Molecules Article Protein–peptide–calcium phosphate composites were developed for achieving sustainable and controlled protein release. Bovine serum albumin (BSA) as a model acidic protein was efficiently encapsulated with basic polypeptides such as polylysine and polyarginine during the precipitation of calcium phosphate (CaP). The prepared composites were fully characterized in terms of their morphologies, crystallinities, and the porosity of their structures, and from these analyses, it was observed that there are no significant differences between the composites. Scanning transmission electron microscopy and energy dispersive X-ray spectroscopy analysis indicated a homogeneous distribution of nitrogen and sulfur, confirming the uniform distribution of BSA and polypeptide in the CaP composite. In vitro release studies demonstrated that the composite prepared with the peptides α-polylysine and polyarginine were suitable for the gradual release of the protein BSA, while those containing ε-polylysine and no peptide were unsuitable for protein release. Additionally, these composites showed high hemocompatibility for mouse red blood cells, and the osteoblast-like cell proliferation and spread in media with the composites prepared using BSA and α-polylysine showed similar tendencies to medium with no composite. From these results, protein–peptide–CaP composites are expected to be useful as highly biocompatible protein delivery agents. MDPI 2020-05-14 /pmc/articles/PMC7287863/ /pubmed/32423135 http://dx.doi.org/10.3390/molecules25102312 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kato, Katsuya Lee, Sungho Nagata, Fukue Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title | Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title_full | Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title_fullStr | Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title_full_unstemmed | Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title_short | Preparation of Protein–Peptide–Calcium Phosphate Composites for Controlled Protein Release |
title_sort | preparation of protein–peptide–calcium phosphate composites for controlled protein release |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7287863/ https://www.ncbi.nlm.nih.gov/pubmed/32423135 http://dx.doi.org/10.3390/molecules25102312 |
work_keys_str_mv | AT katokatsuya preparationofproteinpeptidecalciumphosphatecompositesforcontrolledproteinrelease AT leesungho preparationofproteinpeptidecalciumphosphatecompositesforcontrolledproteinrelease AT nagatafukue preparationofproteinpeptidecalciumphosphatecompositesforcontrolledproteinrelease |