A novel lipase-catalyzed method for preparing ELR-based bioconjugates
Producción Científica Herein we present a novel one-pot method for the chemical modification of elastin-like recombinamers (ELRs) in a mild and efficient manner involving enzymatic catalysis with Candida antarctica lipase B. The introduction of different functionalities into such ELRs could open up...
Published in: | International Journal of Biological Macromolecules |
---|---|
Main Authors: | , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Elsevier
2019
|
Subjects: | |
Online Access: | http://uvadoc.uva.es/handle/10324/33510 https://doi.org/10.1016/j.ijbiomac.2018.10.028 |
id |
ftunivvalladolid:oai:uvadoc.uva.es:10324/33510 |
---|---|
record_format |
openpolar |
spelling |
ftunivvalladolid:oai:uvadoc.uva.es:10324/33510 2023-05-15T14:03:42+02:00 A novel lipase-catalyzed method for preparing ELR-based bioconjugates Testera Gorgojo, Ana María Santos García, María Mercedes Girotti, Alessandra Arias Vallejo, Francisco Javier Báñez Sanz, José Manuel Alonso Rodrigo, Matilde Rodríguez Cabello, José Carlos 2019 application/pdf http://uvadoc.uva.es/handle/10324/33510 https://doi.org/10.1016/j.ijbiomac.2018.10.028 eng eng Elsevier https://www.sciencedirect.com/science/article/pii/S0141813018334305 https://doi.org/10.1016/j.ijbiomac.2018.10.028 International Journal of Biological Macromolecules, 2019, Volume 121, Pages 752-759 0141-8130 http://uvadoc.uva.es/handle/10324/33510 info:eu-repo/semantics/openAccess © 2018 Elsevier Elastina Modificación enzimática Elastine Enzymatic modification info:eu-repo/semantics/article 2019 ftunivvalladolid https://doi.org/10.1016/j.ijbiomac.2018.10.028 2022-03-10T16:39:15Z Producción Científica Herein we present a novel one-pot method for the chemical modification of elastin-like recombinamers (ELRs) in a mild and efficient manner involving enzymatic catalysis with Candida antarctica lipase B. The introduction of different functionalities into such ELRs could open up new possibilities for the development of advanced biomaterials for regenerative medicine and, specifically, for controlled drug delivery given their additional ability to respond to stimuli other than pH or temperature, such as glucose concentration or electromagnetic radiation. Candida antarctica lipase B immobilized on a macroporous acrylic resin (Novozym 435) was used to enzymatically couple different aminated substrates to a recombinamer containing carboxylic groups along its amino acid chain by way of an amidation reaction. A preliminary study of the kinetics of this amidation in response to different reaction conditions, such as solvent, temperature or reagent ratio, was carried out using a phenylazobenzene derivative (azo-NH2) as a model. The optimal amidation conditions were used to couple other amine reagents, such as phenylboronic acid (FB-NH2) or polyethylene glycol (PEG-NH2), thus allowing us to obtain photoresponsive, glucose-responsive or PEGylated ELRs that could potentially be useful as sensors in devices for controlled drug delivery. 2019-11-11 2019-11-11 European Social Fund (ESF) and European Regional Development Fund (ERDF) Comisión Europea (proyectos NMP-2014-646075, HEALTH-F4-2011-278557, PITN-GA-2012-317306 y MSCA-ITN-2014-642687), Ministerio de Economía, Industria y Competitividad (Projects MAT2015-68901-R, MAT2016-79435-R and MAT2016-78903-R) Junta de Castilla y León (programa de apoyo a proyectos de investigación – Ref. VA244U13 y VA313U14) CIBER-BBN, Instituto de Salud Carlos III a través de la Red de Medicina Regenerativa y Terapia Celular de Castilla y León, Novozymes® Article in Journal/Newspaper Antarc* Antarctica UVaDOC - Repositorio Documental de la Universidad de Valladolid International Journal of Biological Macromolecules 121 752 759 |
institution |
Open Polar |
collection |
UVaDOC - Repositorio Documental de la Universidad de Valladolid |
op_collection_id |
ftunivvalladolid |
language |
English |
topic |
Elastina Modificación enzimática Elastine Enzymatic modification |
spellingShingle |
Elastina Modificación enzimática Elastine Enzymatic modification Testera Gorgojo, Ana María Santos García, María Mercedes Girotti, Alessandra Arias Vallejo, Francisco Javier Báñez Sanz, José Manuel Alonso Rodrigo, Matilde Rodríguez Cabello, José Carlos A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
topic_facet |
Elastina Modificación enzimática Elastine Enzymatic modification |
description |
Producción Científica Herein we present a novel one-pot method for the chemical modification of elastin-like recombinamers (ELRs) in a mild and efficient manner involving enzymatic catalysis with Candida antarctica lipase B. The introduction of different functionalities into such ELRs could open up new possibilities for the development of advanced biomaterials for regenerative medicine and, specifically, for controlled drug delivery given their additional ability to respond to stimuli other than pH or temperature, such as glucose concentration or electromagnetic radiation. Candida antarctica lipase B immobilized on a macroporous acrylic resin (Novozym 435) was used to enzymatically couple different aminated substrates to a recombinamer containing carboxylic groups along its amino acid chain by way of an amidation reaction. A preliminary study of the kinetics of this amidation in response to different reaction conditions, such as solvent, temperature or reagent ratio, was carried out using a phenylazobenzene derivative (azo-NH2) as a model. The optimal amidation conditions were used to couple other amine reagents, such as phenylboronic acid (FB-NH2) or polyethylene glycol (PEG-NH2), thus allowing us to obtain photoresponsive, glucose-responsive or PEGylated ELRs that could potentially be useful as sensors in devices for controlled drug delivery. 2019-11-11 2019-11-11 European Social Fund (ESF) and European Regional Development Fund (ERDF) Comisión Europea (proyectos NMP-2014-646075, HEALTH-F4-2011-278557, PITN-GA-2012-317306 y MSCA-ITN-2014-642687), Ministerio de Economía, Industria y Competitividad (Projects MAT2015-68901-R, MAT2016-79435-R and MAT2016-78903-R) Junta de Castilla y León (programa de apoyo a proyectos de investigación – Ref. VA244U13 y VA313U14) CIBER-BBN, Instituto de Salud Carlos III a través de la Red de Medicina Regenerativa y Terapia Celular de Castilla y León, Novozymes® |
format |
Article in Journal/Newspaper |
author |
Testera Gorgojo, Ana María Santos García, María Mercedes Girotti, Alessandra Arias Vallejo, Francisco Javier Báñez Sanz, José Manuel Alonso Rodrigo, Matilde Rodríguez Cabello, José Carlos |
author_facet |
Testera Gorgojo, Ana María Santos García, María Mercedes Girotti, Alessandra Arias Vallejo, Francisco Javier Báñez Sanz, José Manuel Alonso Rodrigo, Matilde Rodríguez Cabello, José Carlos |
author_sort |
Testera Gorgojo, Ana María |
title |
A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
title_short |
A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
title_full |
A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
title_fullStr |
A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
title_full_unstemmed |
A novel lipase-catalyzed method for preparing ELR-based bioconjugates |
title_sort |
novel lipase-catalyzed method for preparing elr-based bioconjugates |
publisher |
Elsevier |
publishDate |
2019 |
url |
http://uvadoc.uva.es/handle/10324/33510 https://doi.org/10.1016/j.ijbiomac.2018.10.028 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
https://www.sciencedirect.com/science/article/pii/S0141813018334305 https://doi.org/10.1016/j.ijbiomac.2018.10.028 International Journal of Biological Macromolecules, 2019, Volume 121, Pages 752-759 0141-8130 http://uvadoc.uva.es/handle/10324/33510 |
op_rights |
info:eu-repo/semantics/openAccess © 2018 Elsevier |
op_doi |
https://doi.org/10.1016/j.ijbiomac.2018.10.028 |
container_title |
International Journal of Biological Macromolecules |
container_volume |
121 |
container_start_page |
752 |
op_container_end_page |
759 |
_version_ |
1766274508734332928 |