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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/195355
Ver los metadatos del registro completo
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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 |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/ info:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/ |
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 application/pdf |
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) 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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score |
13.070432 |