Effects of probe pollutants on morphological and mechanical measurements of muscle and collagen fibers using atomic force microscopy

Zhu, Jie; Sabharwal, Tanya; Guo, Lian-Hong; Lee, Jenny; Wang, Lin; Wang, Guodong

doi:10.1002/sca.20178

Cited by 3 publications

(2 citation statements)

References 31 publications

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“…I rather than type II collagen fibrils from AC (3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Recently, the nanomechanical properties of AC collagen fibrils were examined in various animal models and human OA specimens via atomic force microscopy (AFM) nanoindentation (18)(19)(20). Stiffening of collagen fibrils meshwork was identified as an early biomarker for the onset of OA.…”

Section: Introductionmentioning

confidence: 99%

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

et al. 2014

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Osteoarthritis (OA) is a prevalent and deliberating joint disorder, which acts as the leading cause for the disability and poor quality of life of the middle-age and elderly people. It is generally believed that OA is degeneration of articular cartilage. However, the debate remains on the role of subchondral bone in pathogenesis of OA. In this study, the nanostiffness of collagen fibrils from articular cartilage in patients with entirely different bone metabolism, that is, OA, osteoporosis (OP), and health, was quantitatively measured with AFM nanoindentation technique. It was found that the stiffness of individual collagen fibril from healthy cartilage was 2.67 ± 0.12GPa under ambient condition and 11.24 ± 0.74MPa in hydrated state respectively. The collagen fibrils were softer in osteoporosis (OP) group (ambient: 1.64 ± 0.12GPa; hydrated: 8.59 ± 0.59MPa). By contrast, the extracted fibrils from OA cartilages were stiffer (ambient: 4.65 ± 0.25GPa; hydrated: 17.26 ± 1.77MPa). The results obtained demonstrated that the collagen fibrils extracted from OA patients are stiffer than those from healthy patients, and therefore the nanomechanical characterization of extracted collagen fibrils may be a promising way for early diagnosis of OA.

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Section: Introductionmentioning

confidence: 99%

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

et al. 2014

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“…Height and error images in 512 × 512 pixels were collected simultaneously to be flattened, erased, and analyzed using AFM image processing offline software NanoScope Analysis V1.10 (Bruker Co., Santa Barbara, CA) [18]. The qualitative data of collagen fibrils width, height, and root-mean-square (Rms) roughness was recorded as mean ± SE (standard error).…”

Section: Afm Imaging and Data Analysismentioning

confidence: 99%

Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

Song

Wang

Tao

et al. 2017

Journal of Food Quality

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Self-assembly of extracted collagen from swine trotter tendon under different conditions was firstly observed using atomic force microscopy; then the effects of collagen concentration, pH value, and metal ions to the topography of the collagen assembly were analyzed with the height images and section analysis data. Collagen assembly under 0.1 M, 0.2 M, 0.3 M CaCl 2 , and MgCl 2 solutions in different pH values showed significant differences (P < 0.05) in the topographical properties including height, width, and roughness. With the concentration being increased, the width of collagen decreased significantly (P < 0.05). The width of collagen fibers was first increased significantly (P < 0.05) and then decreased with the increasing of pH. The collagen was assembled with network structure on the mica in solution with Ca 2+ ions. However, it had shown uniformed fibrous structure with Mg 2+ ions on the new cleaved mica sheet. In addition, the width of collagen fibrous was 31∼58 nm in solution with Mg 2+ but 21∼50 nm in Ca 2+solution. The self-assembly collagen displayed various potential abilities to construct fibers or membrane on mica surfaces with Ca 2+ ions and Mg 2+ irons. Besides, the result of collagen self-assembly had shown more relations among solution pH value, metal ions, and collagen molecular concentration, which will provide useful information on the control of collagen self-assembly in tissue engineering and food packaging engineering.

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Recent developments in dimensional nanometrology using AFMs

Yacoot

Koenders

2011

Meas. Sci. Technol.

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Scanning probe microscopes, in particular the atomic force microscope (AFM), have developed into sophisticated instruments that, throughout the world, are no longer used just for imaging, but for quantitative measurements. A role of the national measurement institutes has been to provide traceable metrology for these instruments. This paper presents a brief overview as to how this has been achieved, highlights the future requirements for metrology to support developments in AFM technology and describes work in progress to meet this need.

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Effects of probe pollutants on morphological and mechanical measurements of muscle and collagen fibers using atomic force microscopy

Cited by 3 publications

References 31 publications

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

Nanostiffness of Collagen Fibrils Extracted from Osteoarthritic Cartilage Characterized with AFM Nanoindentation

Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

Recent developments in dimensional nanometrology using AFMs

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