Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth

Antifreeze proteins (AFPs) are biopolymers capable of interfering with ice growth. Their antifreeze action is commonly understood considering that the AFPs, by pinning the ice surface, force the crystal–liquid interface to bend forming an ice meniscus, causing an increase in the surface free energy...

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Detalles Bibliográficos
Autores: Bianco, Valentino, Espinosa, Jorge R., Vega De Las Heras, Carlos
Tipo de recurso: artículo
Fecha de publicación:2020
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/6637
Acceso en línea:https://hdl.handle.net/20.500.14352/6637
Access Level:acceso abierto
Palabra clave:Química
Agua
Física (Química)
Informática (Química)
Química física (Química)
23 Química
2303.31 Química del Agua
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oai_identifier_str oai:docta.ucm.es:20.500.14352/6637
network_acronym_str ES
network_name_str España
repository_id_str
spelling Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growthBianco, ValentinoEspinosa, Jorge R.Vega De Las Heras, CarlosQuímicaAguaFísica (Química)Informática (Química)Química física (Química)23 Química2303.31 Química del AguaAntifreeze proteins (AFPs) are biopolymers capable of interfering with ice growth. Their antifreeze action is commonly understood considering that the AFPs, by pinning the ice surface, force the crystal–liquid interface to bend forming an ice meniscus, causing an increase in the surface free energy and resulting in a decrease in the freezing point ΔT max. Here, we present an extensive computational study for a model protein adsorbed on a TIP4P/Ice crystal, computing ΔT max as a function of the average distance d between AFPs, with simulations spanning over 1 μs. First, we show that the lower the d, the larger the ΔT max. Then, we find that the water–ice–protein contact angle along the line ΔT max(d) is always larger than 0○ , and we provide a theoretical interpretation. We compute the curvature radius of the stable solid–liquid interface at a given supercooling ΔT ≤ ΔT max, connecting it with the critical ice nucleus at ΔT. Finally, we discuss the antifreeze capability of AFPs in terms of the protein–water and protein–ice interactions. Our findings establish a unified description of the AFPs in the contest of homogeneous ice nucleation, elucidating key aspects of the antifreeze mechanisms and paving the way for the design of novel ice-controlling materials.American Institute of Physics (AIP)Universidad Complutense de Madrid20202020-01-0120202020-01-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/6637reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/66372026-06-02T12:44:21Z
dc.title.none.fl_str_mv Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
title Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
spellingShingle Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
Bianco, Valentino
Química
Agua
Física (Química)
Informática (Química)
Química física (Química)
23 Química
2303.31 Química del Agua
title_short Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
title_full Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
title_fullStr Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
title_full_unstemmed Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
title_sort Antifreeze proteins and homogeneous nucleation: On the physical determinants impeding ice crystal growth
dc.creator.none.fl_str_mv Bianco, Valentino
Espinosa, Jorge R.
Vega De Las Heras, Carlos
author Bianco, Valentino
author_facet Bianco, Valentino
Espinosa, Jorge R.
Vega De Las Heras, Carlos
author_role author
author2 Espinosa, Jorge R.
Vega De Las Heras, Carlos
author2_role author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv Química
Agua
Física (Química)
Informática (Química)
Química física (Química)
23 Química
2303.31 Química del Agua
topic Química
Agua
Física (Química)
Informática (Química)
Química física (Química)
23 Química
2303.31 Química del Agua
description Antifreeze proteins (AFPs) are biopolymers capable of interfering with ice growth. Their antifreeze action is commonly understood considering that the AFPs, by pinning the ice surface, force the crystal–liquid interface to bend forming an ice meniscus, causing an increase in the surface free energy and resulting in a decrease in the freezing point ΔT max. Here, we present an extensive computational study for a model protein adsorbed on a TIP4P/Ice crystal, computing ΔT max as a function of the average distance d between AFPs, with simulations spanning over 1 μs. First, we show that the lower the d, the larger the ΔT max. Then, we find that the water–ice–protein contact angle along the line ΔT max(d) is always larger than 0○ , and we provide a theoretical interpretation. We compute the curvature radius of the stable solid–liquid interface at a given supercooling ΔT ≤ ΔT max, connecting it with the critical ice nucleus at ΔT. Finally, we discuss the antifreeze capability of AFPs in terms of the protein–water and protein–ice interactions. Our findings establish a unified description of the AFPs in the contest of homogeneous ice nucleation, elucidating key aspects of the antifreeze mechanisms and paving the way for the design of novel ice-controlling materials.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01
2020
2020-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/6637
url https://hdl.handle.net/20.500.14352/6637
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Institute of Physics (AIP)
publisher.none.fl_str_mv American Institute of Physics (AIP)
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869416341028470784
score 15,301603

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