Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy

Autores
Wenz, Jorge Javier
Año de publicación
2019
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Near infrared spectroscopy (NIR) is useful to study the H-bonds network in water systems, which are sensitive to solutes. The less the number and/or the strength of H- bonds, the more the strength of the covalent O-H bonds of water. Hence, they vibrate and absorb radiation at higher frequencies. By taking advantage of this spectral shift water in DMPA membranes with and without one of two steroids, progesterone and 25- hydroxycholesterol, was assessed. Spectra of vesicles of DMPA and DMPA/steroid in MilliQ water (500 μM; 80:20 molar ratio for the steroid-containing samples) between 1100 and 2300 nm were acquired at 10 temperatures in the range 13-58 °C, with a path length of 1 mm. For understanding the tangled spectra, principal component analysis was applied to disclose subtle changes mirroring the alterations in the vibrational energy of the O-H bonds, as an indirect measure of the H-bond network. The analysis encompassed the first overtone of water (centered at 1450/1455 nm) representing signals of overlapping water and O-H stretching bands, as well as a limited portion of 1100-1300 nm. The shift to higher frequencies (i.e. higher energy) of the O-H vibration band with increasing temperatures or in the presence of 25-hydroxycholesterol is consistent with a strengthening of the O-H bonds caused by disruption/weakening of the H-bonds. The number of strongly H-bonded waters decreases whereas the number of weakly H-bonded waters increases. The observed shift agrees with reports about the distinct absorption of three states of water: waters having no -OH bonded, having one -OH group H-bonded and having two -OHs H-bonded. In contrast, DMPA and progesterone did not show significant effects on the H-bonds network. Findings concur with the lipid domain- promoting activity reported for 25-hydroxycholesterol (a cholesterol-like behavior) and with the slightly (or absent) lipid domain-disrupting activity of progesterone.
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
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
Materia
MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
CHEMOMETRICS
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:11336/195355

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spelling Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopyWenz, Jorge JavierMEMBRANESWATERNEAR INFRARED SPECTROSCOPYCHEMOMETRICShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Near infrared spectroscopy (NIR) is useful to study the H-bonds network in water systems, which are sensitive to solutes. The less the number and/or the strength of H- bonds, the more the strength of the covalent O-H bonds of water. Hence, they vibrate and absorb radiation at higher frequencies. By taking advantage of this spectral shift water in DMPA membranes with and without one of two steroids, progesterone and 25- hydroxycholesterol, was assessed. Spectra of vesicles of DMPA and DMPA/steroid in MilliQ water (500 μM; 80:20 molar ratio for the steroid-containing samples) between 1100 and 2300 nm were acquired at 10 temperatures in the range 13-58 °C, with a path length of 1 mm. For understanding the tangled spectra, principal component analysis was applied to disclose subtle changes mirroring the alterations in the vibrational energy of the O-H bonds, as an indirect measure of the H-bond network. The analysis encompassed the first overtone of water (centered at 1450/1455 nm) representing signals of overlapping water and O-H stretching bands, as well as a limited portion of 1100-1300 nm. The shift to higher frequencies (i.e. higher energy) of the O-H vibration band with increasing temperatures or in the presence of 25-hydroxycholesterol is consistent with a strengthening of the O-H bonds caused by disruption/weakening of the H-bonds. The number of strongly H-bonded waters decreases whereas the number of weakly H-bonded waters increases. The observed shift agrees with reports about the distinct absorption of three states of water: waters having no -OH bonded, having one -OH group H-bonded and having two -OHs H-bonded. In contrast, DMPA and progesterone did not show significant effects on the H-bonds network. Findings concur with the lipid domain- promoting activity reported for 25-hydroxycholesterol (a cholesterol-like behavior) and with the slightly (or absent) lipid domain-disrupting activity of progesterone.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; ArgentinaXLVIII Reunión Anual de la Sociedad Argentina de BiofísicaSan LuisArgentinaSociedad Argentina de BiofísicaSociedad Argentina de BiofísicaAndujar, Sebastian Antonio2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/195355Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 83-83978-987-27591-7-9CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:47:23Zoai:ri.conicet.gov.ar:11336/195355instacron: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 10:47:23.755CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
title Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
spellingShingle Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
Wenz, Jorge Javier
MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
CHEMOMETRICS
title_short Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
title_full Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
title_fullStr Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
title_full_unstemmed Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
title_sort Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy
dc.creator.none.fl_str_mv Wenz, Jorge Javier
author Wenz, Jorge Javier
author_facet Wenz, Jorge Javier
author_role author
dc.contributor.none.fl_str_mv Andujar, Sebastian Antonio
dc.subject.none.fl_str_mv MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
CHEMOMETRICS
topic MEMBRANES
WATER
NEAR INFRARED SPECTROSCOPY
CHEMOMETRICS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Near infrared spectroscopy (NIR) is useful to study the H-bonds network in water systems, which are sensitive to solutes. The less the number and/or the strength of H- bonds, the more the strength of the covalent O-H bonds of water. Hence, they vibrate and absorb radiation at higher frequencies. By taking advantage of this spectral shift water in DMPA membranes with and without one of two steroids, progesterone and 25- hydroxycholesterol, was assessed. Spectra of vesicles of DMPA and DMPA/steroid in MilliQ water (500 μM; 80:20 molar ratio for the steroid-containing samples) between 1100 and 2300 nm were acquired at 10 temperatures in the range 13-58 °C, with a path length of 1 mm. For understanding the tangled spectra, principal component analysis was applied to disclose subtle changes mirroring the alterations in the vibrational energy of the O-H bonds, as an indirect measure of the H-bond network. The analysis encompassed the first overtone of water (centered at 1450/1455 nm) representing signals of overlapping water and O-H stretching bands, as well as a limited portion of 1100-1300 nm. The shift to higher frequencies (i.e. higher energy) of the O-H vibration band with increasing temperatures or in the presence of 25-hydroxycholesterol is consistent with a strengthening of the O-H bonds caused by disruption/weakening of the H-bonds. The number of strongly H-bonded waters decreases whereas the number of weakly H-bonded waters increases. The observed shift agrees with reports about the distinct absorption of three states of water: waters having no -OH bonded, having one -OH group H-bonded and having two -OHs H-bonded. In contrast, DMPA and progesterone did not show significant effects on the H-bonds network. Findings concur with the lipid domain- promoting activity reported for 25-hydroxycholesterol (a cholesterol-like behavior) and with the slightly (or absent) lipid domain-disrupting activity of progesterone.
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
XLVIII Reunión Anual de la Sociedad Argentina de Biofísica
San Luis
Argentina
Sociedad Argentina de Biofísica
description Near infrared spectroscopy (NIR) is useful to study the H-bonds network in water systems, which are sensitive to solutes. The less the number and/or the strength of H- bonds, the more the strength of the covalent O-H bonds of water. Hence, they vibrate and absorb radiation at higher frequencies. By taking advantage of this spectral shift water in DMPA membranes with and without one of two steroids, progesterone and 25- hydroxycholesterol, was assessed. Spectra of vesicles of DMPA and DMPA/steroid in MilliQ water (500 μM; 80:20 molar ratio for the steroid-containing samples) between 1100 and 2300 nm were acquired at 10 temperatures in the range 13-58 °C, with a path length of 1 mm. For understanding the tangled spectra, principal component analysis was applied to disclose subtle changes mirroring the alterations in the vibrational energy of the O-H bonds, as an indirect measure of the H-bond network. The analysis encompassed the first overtone of water (centered at 1450/1455 nm) representing signals of overlapping water and O-H stretching bands, as well as a limited portion of 1100-1300 nm. The shift to higher frequencies (i.e. higher energy) of the O-H vibration band with increasing temperatures or in the presence of 25-hydroxycholesterol is consistent with a strengthening of the O-H bonds caused by disruption/weakening of the H-bonds. The number of strongly H-bonded waters decreases whereas the number of weakly H-bonded waters increases. The observed shift agrees with reports about the distinct absorption of three states of water: waters having no -OH bonded, having one -OH group H-bonded and having two -OHs H-bonded. In contrast, DMPA and progesterone did not show significant effects on the H-bonds network. Findings concur with the lipid domain- promoting activity reported for 25-hydroxycholesterol (a cholesterol-like behavior) and with the slightly (or absent) lipid domain-disrupting activity of progesterone.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/195355
Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 83-83
978-987-27591-7-9
CONICET Digital
CONICET
url http://hdl.handle.net/11336/195355
identifier_str_mv Hydrogen bonds and water in steroid-containing phospholipidic membranes assessed by near infrared spectroscopy; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; San Luis; Argentina; 2019; 83-83
978-987-27591-7-9
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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