Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications
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Publication Date: | 2021 |
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Format: | Other |
Language: | eng |
Source: | Repositório Institucional da UNESP |
Download full: | http://dx.doi.org/10.1186/s12951-021-00774-y http://hdl.handle.net/11449/208342 |
Summary: | Background: The advances in products based on nanotechnology have directed extensive research on low-cost, biologically compatible, and easily degradable materials. Main body: Sericin (SER) is a protein mainly composed of glycine, serine, aspartic acid, and threonine amino acids removed from the silkworm cocoon (particularly Bombyx mori and other species). SER is a biocompatible material with economic viability, which can be easily functionalized due to its potential crosslink reactions. Also, SER has inherent biological properties, which makes possible its use as a component of pharmaceutical formulations with several biomedical applications, such as anti-tumor, antimicrobials, antioxidants and as scaffolds for tissue repair as well as participating in molecular mechanisms attributed to the regulation of transcription factors, reduction of inflammatory signaling molecules, stimulation of apoptosis, migration, and proliferation of mesenchymal cells. Conclusion: In this review, the recent innovations on SER-based nano-medicines (nanoparticles, micelles, films, hydrogels, and their hybrid systems) and their contributions for non-conventional therapies are discussed considering different molecular mechanisms for promoting their therapeutic applications.[Figure not available: see fulltext.] |
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Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applicationsBiomaterialsBiomedicalDrug deliveryNanoformulationSericinSilk proteinBackground: The advances in products based on nanotechnology have directed extensive research on low-cost, biologically compatible, and easily degradable materials. Main body: Sericin (SER) is a protein mainly composed of glycine, serine, aspartic acid, and threonine amino acids removed from the silkworm cocoon (particularly Bombyx mori and other species). SER is a biocompatible material with economic viability, which can be easily functionalized due to its potential crosslink reactions. Also, SER has inherent biological properties, which makes possible its use as a component of pharmaceutical formulations with several biomedical applications, such as anti-tumor, antimicrobials, antioxidants and as scaffolds for tissue repair as well as participating in molecular mechanisms attributed to the regulation of transcription factors, reduction of inflammatory signaling molecules, stimulation of apoptosis, migration, and proliferation of mesenchymal cells. Conclusion: In this review, the recent innovations on SER-based nano-medicines (nanoparticles, micelles, films, hydrogels, and their hybrid systems) and their contributions for non-conventional therapies are discussed considering different molecular mechanisms for promoting their therapeutic applications.[Figure not available: see fulltext.]National Research Foundation of KoreaResearch Institute of Biotechnology & Medical Converged Science Dongguk University-SeoulDepartment of Food Science & Biotechnology Dongguk University-SeoulHuman and Natural Sciences Center Federal University of ABC. Av. Dos Estados, 5001. Bl. A, T3, Lab. 503-3. BangúInstitute of Science and Technology of Sorocaba São Paulo State University (UNESP), Av. Três de março, 511, Alto da Boa VistaDepartamento de Ingenieria Molecular de Materiales Centro de Fisica Aplicada y Tecnologia Avanzada Universidad Nacional Autonoma de Mexico, Blvd. Juriquilla 3001Sustainability of Natural Resources and Energy Programs, Cinvestav-SaltilloDepartment of Physics and Chemistry São Paulo State University (UNESP), Avenida Brasil, 56, CentroInstitute of Science and Technology of Sorocaba São Paulo State University (UNESP), Av. Três de março, 511, Alto da Boa VistaDepartment of Physics and Chemistry São Paulo State University (UNESP), Avenida Brasil, 56, CentroNational Research Foundation of Korea: 2020R1G1A1004667Dongguk University-SeoulFederal University of ABC. Av. Dos EstadosUniversidade Estadual Paulista (Unesp)Universidad Nacional Autonoma de MexicoSustainability of Natural Resources and Energy ProgramsDas, GitishreeShin, Han-SeungCampos, Estefânia V. RamosFraceto, Leonardo Fernandes [UNESP]del Pilar Rodriguez-Torres, MariaMariano, Kelli Cristina Freitasde Araujo, Daniele RibeiroFernández-Luqueño, FabiánGrillo, Renato [UNESP]Patra, Jayanta Kumar2021-06-25T11:10:34Z2021-06-25T11:10:34Z2021-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/otherhttp://dx.doi.org/10.1186/s12951-021-00774-yJournal of Nanobiotechnology, v. 19, n. 1, 2021.1477-3155http://hdl.handle.net/11449/20834210.1186/s12951-021-00774-y2-s2.0-85099793128Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Nanobiotechnologyinfo:eu-repo/semantics/openAccess2024-11-21T13:11:21Zoai:repositorio.unesp.br:11449/208342Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestrepositoriounesp@unesp.bropendoar:29462024-11-21T13:11:21Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
title |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
spellingShingle |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications Das, Gitishree Biomaterials Biomedical Drug delivery Nanoformulation Sericin Silk protein |
title_short |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
title_full |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
title_fullStr |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
title_full_unstemmed |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
title_sort |
Sericin based nanoformulations: a comprehensive review on molecular mechanisms of interaction with organisms to biological applications |
author |
Das, Gitishree |
author_facet |
Das, Gitishree Shin, Han-Seung Campos, Estefânia V. Ramos Fraceto, Leonardo Fernandes [UNESP] del Pilar Rodriguez-Torres, Maria Mariano, Kelli Cristina Freitas de Araujo, Daniele Ribeiro Fernández-Luqueño, Fabián Grillo, Renato [UNESP] Patra, Jayanta Kumar |
author_role |
author |
author2 |
Shin, Han-Seung Campos, Estefânia V. Ramos Fraceto, Leonardo Fernandes [UNESP] del Pilar Rodriguez-Torres, Maria Mariano, Kelli Cristina Freitas de Araujo, Daniele Ribeiro Fernández-Luqueño, Fabián Grillo, Renato [UNESP] Patra, Jayanta Kumar |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Dongguk University-Seoul Federal University of ABC. Av. Dos Estados Universidade Estadual Paulista (Unesp) Universidad Nacional Autonoma de Mexico Sustainability of Natural Resources and Energy Programs |
dc.contributor.author.fl_str_mv |
Das, Gitishree Shin, Han-Seung Campos, Estefânia V. Ramos Fraceto, Leonardo Fernandes [UNESP] del Pilar Rodriguez-Torres, Maria Mariano, Kelli Cristina Freitas de Araujo, Daniele Ribeiro Fernández-Luqueño, Fabián Grillo, Renato [UNESP] Patra, Jayanta Kumar |
dc.subject.por.fl_str_mv |
Biomaterials Biomedical Drug delivery Nanoformulation Sericin Silk protein |
topic |
Biomaterials Biomedical Drug delivery Nanoformulation Sericin Silk protein |
description |
Background: The advances in products based on nanotechnology have directed extensive research on low-cost, biologically compatible, and easily degradable materials. Main body: Sericin (SER) is a protein mainly composed of glycine, serine, aspartic acid, and threonine amino acids removed from the silkworm cocoon (particularly Bombyx mori and other species). SER is a biocompatible material with economic viability, which can be easily functionalized due to its potential crosslink reactions. Also, SER has inherent biological properties, which makes possible its use as a component of pharmaceutical formulations with several biomedical applications, such as anti-tumor, antimicrobials, antioxidants and as scaffolds for tissue repair as well as participating in molecular mechanisms attributed to the regulation of transcription factors, reduction of inflammatory signaling molecules, stimulation of apoptosis, migration, and proliferation of mesenchymal cells. Conclusion: In this review, the recent innovations on SER-based nano-medicines (nanoparticles, micelles, films, hydrogels, and their hybrid systems) and their contributions for non-conventional therapies are discussed considering different molecular mechanisms for promoting their therapeutic applications.[Figure not available: see fulltext.] |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-06-25T11:10:34Z 2021-06-25T11:10:34Z 2021-12-01 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/other |
format |
other |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1186/s12951-021-00774-y Journal of Nanobiotechnology, v. 19, n. 1, 2021. 1477-3155 http://hdl.handle.net/11449/208342 10.1186/s12951-021-00774-y 2-s2.0-85099793128 |
url |
http://dx.doi.org/10.1186/s12951-021-00774-y http://hdl.handle.net/11449/208342 |
identifier_str_mv |
Journal of Nanobiotechnology, v. 19, n. 1, 2021. 1477-3155 10.1186/s12951-021-00774-y 2-s2.0-85099793128 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Nanobiotechnology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
repositoriounesp@unesp.br |
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1834483230527455232 |