Examining water in model membranes by near infrared spectroscopy and multivariate analysis

Autores
Wenz, Jorge Javier
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
By exploiting the sensitivity of the NIR spectrum, particularly the first overtone of water, to the number and strength of hydrogen bonds, the hydrogen bond network and water polymerization in membranes of DMPA (1,2-dimyristoyl-sn-glycero-3-phosphate) and DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) was investigated as a function of the temperature and the presence of this two phospholipids having the same tail but different polar head. Principal components analysis performed on the spectra was used to disclose subtle spectral changes that mirror the alteration of the vibrational energy of the water O-H bonds, as a measure of the H-bond network. Temperature showed a dominating effect on the H-bond network. Increasing temperatures diminished the number of strongly H-bonded water molecules and increased the number of weakly H-bonded waters. This main effect of temperature was missing after the subtraction of the pure water spectra from the lipid-containing ones. An intriguing secondary effect of temperature was also revealed. Phospholipids exhibited an effect qualitatively similar to that of the temperature. DMPA, and particularly DMPC, disrupted the H-bond network in the neighboring lipid-water interface, reducing water polymerization and strengthening the water O-H bonds. The type of the polar head affects the H-bonds more than duplicate the concentration of the lipid. A connection between head group structure and the effect on the H-bonds network, and the existence of two populations of water molecules are discussed.
Fil: Wenz, Jorge Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Materia
MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
PRINCIPAL COMPONENT ANALYSIS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/85209

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spelling Examining water in model membranes by near infrared spectroscopy and multivariate analysisWenz, Jorge JavierMEMBRANESWATERNEAR INFRARED SPECTROSCOPYPRINCIPAL COMPONENT ANALYSIShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1By exploiting the sensitivity of the NIR spectrum, particularly the first overtone of water, to the number and strength of hydrogen bonds, the hydrogen bond network and water polymerization in membranes of DMPA (1,2-dimyristoyl-sn-glycero-3-phosphate) and DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) was investigated as a function of the temperature and the presence of this two phospholipids having the same tail but different polar head. Principal components analysis performed on the spectra was used to disclose subtle spectral changes that mirror the alteration of the vibrational energy of the water O-H bonds, as a measure of the H-bond network. Temperature showed a dominating effect on the H-bond network. Increasing temperatures diminished the number of strongly H-bonded water molecules and increased the number of weakly H-bonded waters. This main effect of temperature was missing after the subtraction of the pure water spectra from the lipid-containing ones. An intriguing secondary effect of temperature was also revealed. Phospholipids exhibited an effect qualitatively similar to that of the temperature. DMPA, and particularly DMPC, disrupted the H-bond network in the neighboring lipid-water interface, reducing water polymerization and strengthening the water O-H bonds. The type of the polar head affects the H-bonds more than duplicate the concentration of the lipid. A connection between head group structure and the effect on the H-bonds network, and the existence of two populations of water molecules are discussed.Fil: Wenz, Jorge Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaElsevier Science2018-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/85209Wenz, Jorge Javier; Examining water in model membranes by near infrared spectroscopy and multivariate analysis; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1860; 3; 3-2018; 673-6820005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2017.12.007info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273617303905info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:37:57Zoai:ri.conicet.gov.ar:11336/85209instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:37:57.952CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Examining water in model membranes by near infrared spectroscopy and multivariate analysis
title Examining water in model membranes by near infrared spectroscopy and multivariate analysis
spellingShingle Examining water in model membranes by near infrared spectroscopy and multivariate analysis
Wenz, Jorge Javier
MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
PRINCIPAL COMPONENT ANALYSIS
title_short Examining water in model membranes by near infrared spectroscopy and multivariate analysis
title_full Examining water in model membranes by near infrared spectroscopy and multivariate analysis
title_fullStr Examining water in model membranes by near infrared spectroscopy and multivariate analysis
title_full_unstemmed Examining water in model membranes by near infrared spectroscopy and multivariate analysis
title_sort Examining water in model membranes by near infrared spectroscopy and multivariate analysis
dc.creator.none.fl_str_mv Wenz, Jorge Javier
author Wenz, Jorge Javier
author_facet Wenz, Jorge Javier
author_role author
dc.subject.none.fl_str_mv MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
PRINCIPAL COMPONENT ANALYSIS
topic MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
PRINCIPAL COMPONENT ANALYSIS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv By exploiting the sensitivity of the NIR spectrum, particularly the first overtone of water, to the number and strength of hydrogen bonds, the hydrogen bond network and water polymerization in membranes of DMPA (1,2-dimyristoyl-sn-glycero-3-phosphate) and DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) was investigated as a function of the temperature and the presence of this two phospholipids having the same tail but different polar head. Principal components analysis performed on the spectra was used to disclose subtle spectral changes that mirror the alteration of the vibrational energy of the water O-H bonds, as a measure of the H-bond network. Temperature showed a dominating effect on the H-bond network. Increasing temperatures diminished the number of strongly H-bonded water molecules and increased the number of weakly H-bonded waters. This main effect of temperature was missing after the subtraction of the pure water spectra from the lipid-containing ones. An intriguing secondary effect of temperature was also revealed. Phospholipids exhibited an effect qualitatively similar to that of the temperature. DMPA, and particularly DMPC, disrupted the H-bond network in the neighboring lipid-water interface, reducing water polymerization and strengthening the water O-H bonds. The type of the polar head affects the H-bonds more than duplicate the concentration of the lipid. A connection between head group structure and the effect on the H-bonds network, and the existence of two populations of water molecules are discussed.
Fil: Wenz, Jorge Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
description By exploiting the sensitivity of the NIR spectrum, particularly the first overtone of water, to the number and strength of hydrogen bonds, the hydrogen bond network and water polymerization in membranes of DMPA (1,2-dimyristoyl-sn-glycero-3-phosphate) and DMPC (1,2-dimyristoyl-sn-glycero-3-phosphocholine) was investigated as a function of the temperature and the presence of this two phospholipids having the same tail but different polar head. Principal components analysis performed on the spectra was used to disclose subtle spectral changes that mirror the alteration of the vibrational energy of the water O-H bonds, as a measure of the H-bond network. Temperature showed a dominating effect on the H-bond network. Increasing temperatures diminished the number of strongly H-bonded water molecules and increased the number of weakly H-bonded waters. This main effect of temperature was missing after the subtraction of the pure water spectra from the lipid-containing ones. An intriguing secondary effect of temperature was also revealed. Phospholipids exhibited an effect qualitatively similar to that of the temperature. DMPA, and particularly DMPC, disrupted the H-bond network in the neighboring lipid-water interface, reducing water polymerization and strengthening the water O-H bonds. The type of the polar head affects the H-bonds more than duplicate the concentration of the lipid. A connection between head group structure and the effect on the H-bonds network, and the existence of two populations of water molecules are discussed.
publishDate 2018
dc.date.none.fl_str_mv 2018-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/85209
Wenz, Jorge Javier; Examining water in model membranes by near infrared spectroscopy and multivariate analysis; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1860; 3; 3-2018; 673-682
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/85209
identifier_str_mv Wenz, Jorge Javier; Examining water in model membranes by near infrared spectroscopy and multivariate analysis; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1860; 3; 3-2018; 673-682
0005-2736
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2017.12.007
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273617303905
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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