High-resolution AFM imaging of intact and fractured trabecular bone

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High-resolution AFM imaging of intact and fractured trabecular bone. / Hassenkam, Tue; Fantner, Georg E.; Cutroni, Jacqueline A.; Weaver, James C.; Morse, Daniel E.; Hansma, Paul K.

In: Bone, Vol. 35, No. 1, 2004, p. 4-10.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Hassenkam, T, Fantner, GE, Cutroni, JA, Weaver, JC, Morse, DE & Hansma, PK 2004, 'High-resolution AFM imaging of intact and fractured trabecular bone', Bone, vol. 35, no. 1, pp. 4-10. https://doi.org/10.1016/j.bone.2004.02.024

APA

Hassenkam, T., Fantner, G. E., Cutroni, J. A., Weaver, J. C., Morse, D. E., & Hansma, P. K. (2004). High-resolution AFM imaging of intact and fractured trabecular bone. Bone, 35(1), 4-10. https://doi.org/10.1016/j.bone.2004.02.024

Vancouver

Hassenkam T, Fantner GE, Cutroni JA, Weaver JC, Morse DE, Hansma PK. High-resolution AFM imaging of intact and fractured trabecular bone. Bone. 2004;35(1):4-10. https://doi.org/10.1016/j.bone.2004.02.024

Author

Hassenkam, Tue ; Fantner, Georg E. ; Cutroni, Jacqueline A. ; Weaver, James C. ; Morse, Daniel E. ; Hansma, Paul K. / High-resolution AFM imaging of intact and fractured trabecular bone. In: Bone. 2004 ; Vol. 35, No. 1. pp. 4-10.

Bibtex

@article{57ad90ea66544a778e088b3f12511ea7,
title = "High-resolution AFM imaging of intact and fractured trabecular bone",
abstract = "Nanoscale structural analyses of biomineralized materials can frequently help elucidate important structure-function relationships in these complex organic-inorganic composites. Atomic force microscope (AFM) imaging of the exterior surface of trabecular bone reveals a densely woven structure of collagen fibrils, banded with a 67-nm periodicity, and densely packed mineral plates. The mineral plates on the collagen fibrils overlap and exhibit a large range of plate diameters from 30 to 200 nm. On the collagen fibrils, small nodular features, spaced 20-30 nm, run perpendicular to the fibrils. In some cases, these nodules are also seen on filaments extending between collagen fibrils. We hypothesize that these protrusions are noncollagenous proteins such as proteoglycans and may have collapsed into compact structures when the sample was dried. AFM images of pristine fractured surfaces reveal a dense array of mineral plates. In a few isolated locations, short sections of bare collagen fibrils are visible. In other regions, the existence of the underlying collagen fibrils can be inferred from the linear patterns of the mineral plates. Fractured samples, rinsed to remove mineral plates, reveal separated collagen fibrils on the fractured surfaces. These fibrils are often covered with protrusions similar to those observed on the exterior surfaces but are less organized. In addition, as on the exterior surfaces, there are sometimes small filaments extending between neighboring collagen fibrils. These studies provide important insights into the nanostructured architecture of this complex biocomposite.",
keywords = "AFM, Atomic force microscope, Collagen fibrils, Mineral plates, Nanostructure, Trabecular bone",
author = "Tue Hassenkam and Fantner, {Georg E.} and Cutroni, {Jacqueline A.} and Weaver, {James C.} and Morse, {Daniel E.} and Hansma, {Paul K.}",
note = "Funding Information: The research was supported by NASA/URETI on Bio Inspired Materials under award NCC-1-02037, NIH under award GM65354, NSF under award DMR-9988640, a research agreement with Veeco, and the UCSB Materials Research Laboratory under an NSF award DMR00-80034, the Institute for Collaborative Biotechnologies through grant DAAD19-03-D-0004 from the U.S. Army Research Office, and the NOAA National Sea Grant College Program, U.S. Department of Commerce (NA36RG0537, Project R/MP-92) through the California Sea Grant College System, and the Danish research councils (STVF).",
year = "2004",
doi = "10.1016/j.bone.2004.02.024",
language = "English",
volume = "35",
pages = "4--10",
journal = "Bone",
issn = "8756-3282",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - High-resolution AFM imaging of intact and fractured trabecular bone

AU - Hassenkam, Tue

AU - Fantner, Georg E.

AU - Cutroni, Jacqueline A.

AU - Weaver, James C.

AU - Morse, Daniel E.

AU - Hansma, Paul K.

N1 - Funding Information: The research was supported by NASA/URETI on Bio Inspired Materials under award NCC-1-02037, NIH under award GM65354, NSF under award DMR-9988640, a research agreement with Veeco, and the UCSB Materials Research Laboratory under an NSF award DMR00-80034, the Institute for Collaborative Biotechnologies through grant DAAD19-03-D-0004 from the U.S. Army Research Office, and the NOAA National Sea Grant College Program, U.S. Department of Commerce (NA36RG0537, Project R/MP-92) through the California Sea Grant College System, and the Danish research councils (STVF).

PY - 2004

Y1 - 2004

N2 - Nanoscale structural analyses of biomineralized materials can frequently help elucidate important structure-function relationships in these complex organic-inorganic composites. Atomic force microscope (AFM) imaging of the exterior surface of trabecular bone reveals a densely woven structure of collagen fibrils, banded with a 67-nm periodicity, and densely packed mineral plates. The mineral plates on the collagen fibrils overlap and exhibit a large range of plate diameters from 30 to 200 nm. On the collagen fibrils, small nodular features, spaced 20-30 nm, run perpendicular to the fibrils. In some cases, these nodules are also seen on filaments extending between collagen fibrils. We hypothesize that these protrusions are noncollagenous proteins such as proteoglycans and may have collapsed into compact structures when the sample was dried. AFM images of pristine fractured surfaces reveal a dense array of mineral plates. In a few isolated locations, short sections of bare collagen fibrils are visible. In other regions, the existence of the underlying collagen fibrils can be inferred from the linear patterns of the mineral plates. Fractured samples, rinsed to remove mineral plates, reveal separated collagen fibrils on the fractured surfaces. These fibrils are often covered with protrusions similar to those observed on the exterior surfaces but are less organized. In addition, as on the exterior surfaces, there are sometimes small filaments extending between neighboring collagen fibrils. These studies provide important insights into the nanostructured architecture of this complex biocomposite.

AB - Nanoscale structural analyses of biomineralized materials can frequently help elucidate important structure-function relationships in these complex organic-inorganic composites. Atomic force microscope (AFM) imaging of the exterior surface of trabecular bone reveals a densely woven structure of collagen fibrils, banded with a 67-nm periodicity, and densely packed mineral plates. The mineral plates on the collagen fibrils overlap and exhibit a large range of plate diameters from 30 to 200 nm. On the collagen fibrils, small nodular features, spaced 20-30 nm, run perpendicular to the fibrils. In some cases, these nodules are also seen on filaments extending between collagen fibrils. We hypothesize that these protrusions are noncollagenous proteins such as proteoglycans and may have collapsed into compact structures when the sample was dried. AFM images of pristine fractured surfaces reveal a dense array of mineral plates. In a few isolated locations, short sections of bare collagen fibrils are visible. In other regions, the existence of the underlying collagen fibrils can be inferred from the linear patterns of the mineral plates. Fractured samples, rinsed to remove mineral plates, reveal separated collagen fibrils on the fractured surfaces. These fibrils are often covered with protrusions similar to those observed on the exterior surfaces but are less organized. In addition, as on the exterior surfaces, there are sometimes small filaments extending between neighboring collagen fibrils. These studies provide important insights into the nanostructured architecture of this complex biocomposite.

KW - AFM

KW - Atomic force microscope

KW - Collagen fibrils

KW - Mineral plates

KW - Nanostructure

KW - Trabecular bone

U2 - 10.1016/j.bone.2004.02.024

DO - 10.1016/j.bone.2004.02.024

M3 - Journal article

C2 - 15207735

AN - SCOPUS:2942733444

VL - 35

SP - 4

EP - 10

JO - Bone

JF - Bone

SN - 8756-3282

IS - 1

ER -

ID: 288850348