Denaturation processes of collagen from cow bones as a function of temperature

Autores
Lambri, Melania Lucila; Bozzano, Patricia Beatriz; Giordano, Enrique David Victor; Bonifacich, Federico Guillermo; Gargicevich, Damian; Zelada, Griselda Irene; Lambri, Osvaldo Agustin F.
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The thermal stability of collagen is of great interest for the scientific communities both of medicine and archaeology. In medicine, the interest is focused to the reconstruction and repair of bone and cartilage, given the frequency and importance of pathological situations. In contrast, in archaeology the interest is focused to infer from buried and/or burned bones the behavior and habits of people who once inhabited archaeological sites. In bones from cow ribs, the biodegradation of collagen by denaturation of albumin and haemoglobin proteins, the loss of water and the loss of crystallization water during warming up to around 450 K, have been studied. In addition, from an easy-to-handle mathematical viscoelastic procedure, it was determined that the conformational changes from the collagenic triple helix towards the random coil are made through the viscous movement of fibrils, invoking an activation energy of (127 ± 8) kJ/mol. In the present work, the thermal stability of type I collagen from cow bones, either femur and rib, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. In fact, this temperature range is wider than the previous explored ones. Several stages of denaturation were found in the temperature range from 320 K up to 670 K, including also the transition from the triple helix (TH) towards the random coil (RC) of the collagen fibrils. The temperature for the TH → RC transition was approximately the same for all the kinds of bones, but the intensity of the relaxation processes depended upon the kind of bone. The differences between the denaturation processes in the femur and rib are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed. In fact, different behaviours of the mesostructure were found between the cortical parts of bones from ribs and femurs. In addition, the cancellous parts from ribs bone exhibits the survival of organic compounds even at temperatures as higher as 673 K. The results from the present work are crucial both for the tissue engineering, focused to bone replacement and pathologic treatments, and for the archaeology, for the study of identification of buried and/or burned bones in archaeological sites.
Fil: Lambri, Melania Lucila. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bozzano, Patricia Beatriz. Comisión Nacional de Energía Atómica; Argentina
Fil: Giordano, Enrique David Victor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina
Fil: Bonifacich, Federico Guillermo. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gargicevich, Damian. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zelada, Griselda Irene. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina
Fil: Lambri, Osvaldo Agustin F.. Universidad Nacional de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
ARCHAEOMETRY
BONE REPAIR
COW BONES
THERMAL DENATURATION
TISSUE ENGINEERING
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:11336/92690
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/92690
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Denaturation processes of collagen from cow bones as a function of temperatureLambri, Melania LucilaBozzano, Patricia BeatrizGiordano, Enrique David VictorBonifacich, Federico GuillermoGargicevich, DamianZelada, Griselda IreneLambri, Osvaldo Agustin F.ARCHAEOMETRYBONE REPAIRCOW BONESTHERMAL DENATURATIONTISSUE ENGINEERINGhttps://purl.org/becyt/ford/2.5https://purl.org/becyt/ford/2The thermal stability of collagen is of great interest for the scientific communities both of medicine and archaeology. In medicine, the interest is focused to the reconstruction and repair of bone and cartilage, given the frequency and importance of pathological situations. In contrast, in archaeology the interest is focused to infer from buried and/or burned bones the behavior and habits of people who once inhabited archaeological sites. In bones from cow ribs, the biodegradation of collagen by denaturation of albumin and haemoglobin proteins, the loss of water and the loss of crystallization water during warming up to around 450 K, have been studied. In addition, from an easy-to-handle mathematical viscoelastic procedure, it was determined that the conformational changes from the collagenic triple helix towards the random coil are made through the viscous movement of fibrils, invoking an activation energy of (127 ± 8) kJ/mol. In the present work, the thermal stability of type I collagen from cow bones, either femur and rib, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. In fact, this temperature range is wider than the previous explored ones. Several stages of denaturation were found in the temperature range from 320 K up to 670 K, including also the transition from the triple helix (TH) towards the random coil (RC) of the collagen fibrils. The temperature for the TH → RC transition was approximately the same for all the kinds of bones, but the intensity of the relaxation processes depended upon the kind of bone. The differences between the denaturation processes in the femur and rib are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed. In fact, different behaviours of the mesostructure were found between the cortical parts of bones from ribs and femurs. In addition, the cancellous parts from ribs bone exhibits the survival of organic compounds even at temperatures as higher as 673 K. The results from the present work are crucial both for the tissue engineering, focused to bone replacement and pathologic treatments, and for the archaeology, for the study of identification of buried and/or burned bones in archaeological sites.Fil: Lambri, Melania Lucila. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bozzano, Patricia Beatriz. Comisión Nacional de Energía Atómica; ArgentinaFil: Giordano, Enrique David Victor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; ArgentinaFil: Bonifacich, Federico Guillermo. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Gargicevich, Damian. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Zelada, Griselda Irene. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; ArgentinaFil: Lambri, Osvaldo Agustin F.. Universidad Nacional de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaUniversidade Federal do Rio de Janeiro2018-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92690Lambri, Melania Lucila; Bozzano, Patricia Beatriz; Giordano, Enrique David Victor; Bonifacich, Federico Guillermo; Gargicevich, Damian; et al.; Denaturation processes of collagen from cow bones as a function of temperature; Universidade Federal do Rio de Janeiro; Matéria; 23; 2; 7-2018; 1-111517-7076CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://ref.scielo.org/4qt3j5info:eu-repo/semantics/altIdentifier/doi/10.1590/S1517-707620180002.0424info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:41:47Zoai:ri.conicet.gov.ar:11336/92690instacron: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 09:41:48.007CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Denaturation processes of collagen from cow bones as a function of temperature
title Denaturation processes of collagen from cow bones as a function of temperature
spellingShingle Denaturation processes of collagen from cow bones as a function of temperature
Lambri, Melania Lucila
ARCHAEOMETRY
BONE REPAIR
COW BONES
THERMAL DENATURATION
TISSUE ENGINEERING
title_short Denaturation processes of collagen from cow bones as a function of temperature
title_full Denaturation processes of collagen from cow bones as a function of temperature
title_fullStr Denaturation processes of collagen from cow bones as a function of temperature
title_full_unstemmed Denaturation processes of collagen from cow bones as a function of temperature
title_sort Denaturation processes of collagen from cow bones as a function of temperature
dc.creator.none.fl_str_mv Lambri, Melania Lucila
Bozzano, Patricia Beatriz
Giordano, Enrique David Victor
Bonifacich, Federico Guillermo
Gargicevich, Damian
Zelada, Griselda Irene
Lambri, Osvaldo Agustin F.
author Lambri, Melania Lucila
author_facet Lambri, Melania Lucila
Bozzano, Patricia Beatriz
Giordano, Enrique David Victor
Bonifacich, Federico Guillermo
Gargicevich, Damian
Zelada, Griselda Irene
Lambri, Osvaldo Agustin F.
author_role author
author2 Bozzano, Patricia Beatriz
Giordano, Enrique David Victor
Bonifacich, Federico Guillermo
Gargicevich, Damian
Zelada, Griselda Irene
Lambri, Osvaldo Agustin F.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv ARCHAEOMETRY
BONE REPAIR
COW BONES
THERMAL DENATURATION
TISSUE ENGINEERING
topic ARCHAEOMETRY
BONE REPAIR
COW BONES
THERMAL DENATURATION
TISSUE ENGINEERING
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.5
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The thermal stability of collagen is of great interest for the scientific communities both of medicine and archaeology. In medicine, the interest is focused to the reconstruction and repair of bone and cartilage, given the frequency and importance of pathological situations. In contrast, in archaeology the interest is focused to infer from buried and/or burned bones the behavior and habits of people who once inhabited archaeological sites. In bones from cow ribs, the biodegradation of collagen by denaturation of albumin and haemoglobin proteins, the loss of water and the loss of crystallization water during warming up to around 450 K, have been studied. In addition, from an easy-to-handle mathematical viscoelastic procedure, it was determined that the conformational changes from the collagenic triple helix towards the random coil are made through the viscous movement of fibrils, invoking an activation energy of (127 ± 8) kJ/mol. In the present work, the thermal stability of type I collagen from cow bones, either femur and rib, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. In fact, this temperature range is wider than the previous explored ones. Several stages of denaturation were found in the temperature range from 320 K up to 670 K, including also the transition from the triple helix (TH) towards the random coil (RC) of the collagen fibrils. The temperature for the TH → RC transition was approximately the same for all the kinds of bones, but the intensity of the relaxation processes depended upon the kind of bone. The differences between the denaturation processes in the femur and rib are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed. In fact, different behaviours of the mesostructure were found between the cortical parts of bones from ribs and femurs. In addition, the cancellous parts from ribs bone exhibits the survival of organic compounds even at temperatures as higher as 673 K. The results from the present work are crucial both for the tissue engineering, focused to bone replacement and pathologic treatments, and for the archaeology, for the study of identification of buried and/or burned bones in archaeological sites.
Fil: Lambri, Melania Lucila. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bozzano, Patricia Beatriz. Comisión Nacional de Energía Atómica; Argentina
Fil: Giordano, Enrique David Victor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina
Fil: Bonifacich, Federico Guillermo. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Gargicevich, Damian. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Zelada, Griselda Irene. Universidad Nacional de Rosario. Facultad de Ciencias Exactas, Ingeniería y Agrimensura; Argentina
Fil: Lambri, Osvaldo Agustin F.. Universidad Nacional de Rosario; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description The thermal stability of collagen is of great interest for the scientific communities both of medicine and archaeology. In medicine, the interest is focused to the reconstruction and repair of bone and cartilage, given the frequency and importance of pathological situations. In contrast, in archaeology the interest is focused to infer from buried and/or burned bones the behavior and habits of people who once inhabited archaeological sites. In bones from cow ribs, the biodegradation of collagen by denaturation of albumin and haemoglobin proteins, the loss of water and the loss of crystallization water during warming up to around 450 K, have been studied. In addition, from an easy-to-handle mathematical viscoelastic procedure, it was determined that the conformational changes from the collagenic triple helix towards the random coil are made through the viscous movement of fibrils, invoking an activation energy of (127 ± 8) kJ/mol. In the present work, the thermal stability of type I collagen from cow bones, either femur and rib, was studied in the temperature range from 250 K up to 670 K by means of dynamic mechanical analysis, scanning electron microscopy and infrared absorption spectroscopy. In fact, this temperature range is wider than the previous explored ones. Several stages of denaturation were found in the temperature range from 320 K up to 670 K, including also the transition from the triple helix (TH) towards the random coil (RC) of the collagen fibrils. The temperature for the TH → RC transition was approximately the same for all the kinds of bones, but the intensity of the relaxation processes depended upon the kind of bone. The differences between the denaturation processes in the femur and rib are highlighted and the physical-chemical mechanisms controlling the denaturation processes are discussed. In fact, different behaviours of the mesostructure were found between the cortical parts of bones from ribs and femurs. In addition, the cancellous parts from ribs bone exhibits the survival of organic compounds even at temperatures as higher as 673 K. The results from the present work are crucial both for the tissue engineering, focused to bone replacement and pathologic treatments, and for the archaeology, for the study of identification of buried and/or burned bones in archaeological sites.
publishDate 2018
dc.date.none.fl_str_mv 2018-07
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/11336/92690
Lambri, Melania Lucila; Bozzano, Patricia Beatriz; Giordano, Enrique David Victor; Bonifacich, Federico Guillermo; Gargicevich, Damian; et al.; Denaturation processes of collagen from cow bones as a function of temperature; Universidade Federal do Rio de Janeiro; Matéria; 23; 2; 7-2018; 1-11
1517-7076
CONICET Digital
CONICET
url http://hdl.handle.net/11336/92690
identifier_str_mv Lambri, Melania Lucila; Bozzano, Patricia Beatriz; Giordano, Enrique David Victor; Bonifacich, Federico Guillermo; Gargicevich, Damian; et al.; Denaturation processes of collagen from cow bones as a function of temperature; Universidade Federal do Rio de Janeiro; Matéria; 23; 2; 7-2018; 1-11
1517-7076
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://ref.scielo.org/4qt3j5
info:eu-repo/semantics/altIdentifier/doi/10.1590/S1517-707620180002.0424
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 Universidade Federal do Rio de Janeiro
publisher.none.fl_str_mv Universidade Federal do Rio de Janeiro
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

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