Nanoscale characterization of acid and thermally treated collagen fibrils

Young Jae Park; Gyu Jin Choi; Se Hwa Kim; Junhee Hahn; Tae Geol Lee; Won Jong Lee; Dae Won Moon

doi:10.1016/j.actbio.2012.05.029

Nanoscale characterization of acid and thermally treated collagen fibrils

Young Jae Park, Gyu Jin Choi, Se Hwa Kim, Junhee Hahn, Tae Geol Lee, Won Jong Lee, Dae Won Moon

Department of New Biology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Type I collagen is a major extracellular matrix component and its hierarchical structure plays an essential role in the regulation of cellular behavior. Here, we have analyzed the changes in the morphological, chemical, and mechanical properties of collagen fibrils induced by acidic and thermal treatments and the influence on the cellular response of MC3T3-E1 cells. Morphological changes induced by the disintegration of the fibrillar structure of collagen were observed using atomic force microscopy. The changes in the surface chemistry due to the disassembly of native collagen fibrils were observed using time-of-flight secondary ion mass spectroscopy (ToF-SIMS). ToF-SIMS spectra were very sensitive to changes in the molecular configuration of the collagen fibrils induced by acidic and thermal treatments due to the extreme surface specificity. In addition, ToF-SIMS showed clear and reproducible changes in the surface amino acid composition corresponding to the acidic and thermal treatments of collagen fibrils. Based on the quantitative map of surface elastic modulus measured by contact-resonance force microscopy, acid and thermally treated collagen showed a lower elastic modulus than native collagen fibrils. Compared with native collagen fibrils, reduced cell spreading and decreased viability of MC3T3-E1 cells were observed on both the acid and thermally treated collagen.

Original language	English
Pages (from-to)	3381-3391
Number of pages	11
Journal	Acta Biomaterialia
Volume	8
Issue number	9
DOIs	https://doi.org/10.1016/j.actbio.2012.05.029
State	Published - Sep 2012

Bibliographical note

Funding Information:
We thank Hyun Kyong Shon and Dae Hyun Kim for technical support. We also thank Changrok Choi for the deposition of plasma-polymerized thin films. This research was supported by grants from the Development of NanoBio Convergence Technology Program of KRISS and the Converging Research Center Program ( 2011K000887 ) through Korean MEST.

Keywords

AFM (atomic force microscopy)
Acidic and thermal treatment
CR-FM (contact-resonance force microscopy)
Collagen fibril
ToF-SIMS (time-of-flight secondary ion mass spectroscopy)

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10.1016/j.actbio.2012.05.029

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title = "Nanoscale characterization of acid and thermally treated collagen fibrils",

abstract = "Type I collagen is a major extracellular matrix component and its hierarchical structure plays an essential role in the regulation of cellular behavior. Here, we have analyzed the changes in the morphological, chemical, and mechanical properties of collagen fibrils induced by acidic and thermal treatments and the influence on the cellular response of MC3T3-E1 cells. Morphological changes induced by the disintegration of the fibrillar structure of collagen were observed using atomic force microscopy. The changes in the surface chemistry due to the disassembly of native collagen fibrils were observed using time-of-flight secondary ion mass spectroscopy (ToF-SIMS). ToF-SIMS spectra were very sensitive to changes in the molecular configuration of the collagen fibrils induced by acidic and thermal treatments due to the extreme surface specificity. In addition, ToF-SIMS showed clear and reproducible changes in the surface amino acid composition corresponding to the acidic and thermal treatments of collagen fibrils. Based on the quantitative map of surface elastic modulus measured by contact-resonance force microscopy, acid and thermally treated collagen showed a lower elastic modulus than native collagen fibrils. Compared with native collagen fibrils, reduced cell spreading and decreased viability of MC3T3-E1 cells were observed on both the acid and thermally treated collagen.",

keywords = "AFM (atomic force microscopy), Acidic and thermal treatment, CR-FM (contact-resonance force microscopy), Collagen fibril, ToF-SIMS (time-of-flight secondary ion mass spectroscopy)",

author = "Park, {Young Jae} and Choi, {Gyu Jin} and Kim, {Se Hwa} and Junhee Hahn and Lee, {Tae Geol} and Lee, {Won Jong} and Moon, {Dae Won}",

note = "Funding Information: We thank Hyun Kyong Shon and Dae Hyun Kim for technical support. We also thank Changrok Choi for the deposition of plasma-polymerized thin films. This research was supported by grants from the Development of NanoBio Convergence Technology Program of KRISS and the Converging Research Center Program ( 2011K000887 ) through Korean MEST. ",

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AU - Choi, Gyu Jin

AU - Kim, Se Hwa

AU - Hahn, Junhee

AU - Lee, Tae Geol

AU - Lee, Won Jong

AU - Moon, Dae Won

N1 - Funding Information: We thank Hyun Kyong Shon and Dae Hyun Kim for technical support. We also thank Changrok Choi for the deposition of plasma-polymerized thin films. This research was supported by grants from the Development of NanoBio Convergence Technology Program of KRISS and the Converging Research Center Program ( 2011K000887 ) through Korean MEST.

PY - 2012/9

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N2 - Type I collagen is a major extracellular matrix component and its hierarchical structure plays an essential role in the regulation of cellular behavior. Here, we have analyzed the changes in the morphological, chemical, and mechanical properties of collagen fibrils induced by acidic and thermal treatments and the influence on the cellular response of MC3T3-E1 cells. Morphological changes induced by the disintegration of the fibrillar structure of collagen were observed using atomic force microscopy. The changes in the surface chemistry due to the disassembly of native collagen fibrils were observed using time-of-flight secondary ion mass spectroscopy (ToF-SIMS). ToF-SIMS spectra were very sensitive to changes in the molecular configuration of the collagen fibrils induced by acidic and thermal treatments due to the extreme surface specificity. In addition, ToF-SIMS showed clear and reproducible changes in the surface amino acid composition corresponding to the acidic and thermal treatments of collagen fibrils. Based on the quantitative map of surface elastic modulus measured by contact-resonance force microscopy, acid and thermally treated collagen showed a lower elastic modulus than native collagen fibrils. Compared with native collagen fibrils, reduced cell spreading and decreased viability of MC3T3-E1 cells were observed on both the acid and thermally treated collagen.

AB - Type I collagen is a major extracellular matrix component and its hierarchical structure plays an essential role in the regulation of cellular behavior. Here, we have analyzed the changes in the morphological, chemical, and mechanical properties of collagen fibrils induced by acidic and thermal treatments and the influence on the cellular response of MC3T3-E1 cells. Morphological changes induced by the disintegration of the fibrillar structure of collagen were observed using atomic force microscopy. The changes in the surface chemistry due to the disassembly of native collagen fibrils were observed using time-of-flight secondary ion mass spectroscopy (ToF-SIMS). ToF-SIMS spectra were very sensitive to changes in the molecular configuration of the collagen fibrils induced by acidic and thermal treatments due to the extreme surface specificity. In addition, ToF-SIMS showed clear and reproducible changes in the surface amino acid composition corresponding to the acidic and thermal treatments of collagen fibrils. Based on the quantitative map of surface elastic modulus measured by contact-resonance force microscopy, acid and thermally treated collagen showed a lower elastic modulus than native collagen fibrils. Compared with native collagen fibrils, reduced cell spreading and decreased viability of MC3T3-E1 cells were observed on both the acid and thermally treated collagen.

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KW - Acidic and thermal treatment

KW - CR-FM (contact-resonance force microscopy)

KW - Collagen fibril

KW - ToF-SIMS (time-of-flight secondary ion mass spectroscopy)

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Nanoscale characterization of acid and thermally treated collagen fibrils

Abstract

Bibliographical note

Keywords

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