Browsing by Subject "AFM"

Now showing 1 - 6 of 6
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    Cholesterol-Induced Buckling in Physisorbed Polymer-Tethered Lipid Monolayers
    (MDPI, 2013-04-06) Hussain, Noor F.; Siegel, Amanda P.; Johnson, Merrell A.; Naumann, Christoph A.; Chemistry and Chemical Biology, School of Science
    The influence of cholesterol concentration on the formation of buckling structures is studied in a physisorbed polymer-tethered lipid monolayer system using epifluorescence microscopy (EPI) and atomic force microscopy (AFM). The monolayer system, built using the Langmuir-Blodgett (LB) technique, consists of 3 mol % poly(ethylene glycol) (PEG) lipopolymers and various concentrations of the phospholipid, 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC), and cholesterol (CHOL). In the absence of CHOL, AFM micrographs show only occasional buckling structures, which is caused by the presence of the lipopolymers in the monolayer. In contrast, a gradual increase of CHOL concentration in the range of 0–40 mol % leads to fascinating film stress relaxation phenomena in the form of enhanced membrane buckling. Buckling structures are moderately deficient in CHOL, but do not cause any notable phospholipid-lipopolymer phase separation. Our experiments demonstrate that membrane buckling in physisorbed polymer-tethered membranes can be controlled through CHOL-mediated adjustment of membrane elastic properties. They further show that CHOL may have a notable impact on molecular confinement in the presence of crowding agents, such as lipopolymers. Our results are significant, because they offer an intriguing prospective on the role of CHOL on the material properties in complex membrane architecture.
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    Distribution of Type I Collagen Morphologies in Bone: Relation to Estrogen Depletion
    (2010-05) Wallace, Joseph M.; Erickson, Blake; Les, Clifford M.; Orr, Bradford G.; Banaszak Holl, Mark M.
    Bone is an amazing material evolved by nature to elegantly balance structural and metabolic needs in the body. Bone health is an integral part of overall health, but our lack of understanding of the ultrastructure of healthy bone precludes us from knowing how disease may impact nanoscale properties in this biological material. Here, we show that quantitative assessments of a distribution of Type I collagen fibril morphologies can be made using atomic force microscopy (AFM). We demonstrate that normal bone contains a distribution of collagen fibril morphologies and that changes in this distribution can be directly related to disease state. Specifically, by monitoring changes in the collagen fibril distribution of sham-operated and estrogen-depleted sheep, we have shown the ability to detect estrogen-deficiency-induced changes in Type I collagen in bone. This discovery provides new insight into the ultrastructure of bone as a tissue and the role of material structure in bone disease. The observation offers the possibility of a much-needed in vitro procedure to complement the current methods used to diagnose osteoporosis and other bone disease.
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    Effects of tissue hydration on nanoscale structural morphology and mechanics of individual Type I collagen fibrils in the Brtl mouse model of Osteogenesis Imperfecta
    (2012-12) Kemp, Arika D.; Harding, Chad C.; Cabral, Wayne A.; Marini, Joan C.; Wallace, Joseph M.
    Type I collagen is the most abundant protein in mammals, and is a vital part of the extracellular matrix for numerous tissues. Despite collagen’s importance, little is known about its nanoscale morphology in tissues and how morphology relates to mechanical function. This study probes nanoscale structure and mechanical properties of collagen as a function of disease in native hydrated tendons. Wild type tendon and tendon from the Brtl/+ mouse model of Osteogenesis Imperfecta were investigated. An atomic force microscope (AFM) was used to image and indent minimally-processed collagen fibrils in hydrated and dehydrated conditions. AFM was used because of the ability to keep biological tissues as close to their native in situ conditions as possible. The study demonstrated phenotypic difference in Brtl/+ fibril morphology and mechanics in hydrated tendon which became more compelling upon dehydration. Dried tendons had a significant downward shift in fibril D- periodic spacing versus a shift up in wet tendons. Nanoscale changes in morphology in dry samples were accompanied by significant increases in modulus and adhesion force and decreased indentation depth. A minimal mechanical phenotype existed in hydrated samples, possibly due to water masking structural defects within the diseased fibrils. This study demonstrates that collagen nanoscale morphology and mechanics are impacted in Brtl/+ tendons, and that the phenotype can be modulated by the presence or absence of water. Dehydration causes artifacts in biological samples which require water and this factor must be considered for studies at any length scale in collagen-based tissues, especially when characterizing disease- induced differences.
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    Experimental Study of Material Removal at Nanoscale
    (Elsevier, 2018-01-01) Promyoo, Rapeepan; El-Mounayri, Hazim; Agarwal, Mangilal; Mechanical Engineering, School of Engineering and Technology
    In order to develop nano-machining into a viable and efficient process, there is a need to achieve a better understand the relation between process parameters (such as feed, speed, and depth of cut) and resulting geometry. In this study, a comprehensive experimental parametric study was conducted to produce a database that is used to select proper machining conditions for guiding the fabrication of precise nano-geometries. The parametric studies conducted using AFM nanosize tips showed the following: normal forces for both nano-indentation and nano-scratching increase as the depth of cut increases. The indentation depth increases with tip speed, but the depth of scratch decrease with increasing tip speed. The width and depth of scratched groove also depend on the scratch angle. The recommended scratch angle is at 90°. The surface roughness increases with step over, especially when the step over is larger than the tip radius. The depth of cut also increases as the step over decreases.
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    Multiscale analysis of morphology and mechanics in tail tendon from the ZDSD rat model of type 2 diabetes
    (2014-02) Gonzalez, Armando Diaz; Gallant, Maxime A.; Burr, David B.; Wallace, Joseph M.
    Type 2 diabetes (T2D) impacts multiple organ systems including the circulatory, renal, nervous and musculoskeletal systems. In collagen-based tissues, one mechanism that may be responsible for detrimental mechanical impacts of T2D is the formation of advanced glycation end products (AGEs) leading to increased collagen stiffness and decreased toughness, resulting in brittle tissue behavior. The purpose of this study was to investigate tendon mechanical properties from normal and diabetic rats at two distinct length scales, testing the hypothesis that increased stiffness and strength and decreased toughness at the fiber level would be associated with alterations in nanoscale morphology and mechanics. Individual fascicles from female Zucker diabetic Sprague-Dawley (ZDSD) rats had no differences in fascicle-level mechanical properties but had increased material-level strength and stiffness versus control rats (CD). At the nanoscale, collagen fibril D-spacing was shifted towards higher spacing values in diabetic ZDSD fibrils. The distribution of nanoscale modulus values was also shifted to higher values. Material-level strength and stiffness from whole fiber tests were increased in ZDSD tails. Correlations between nanoscale and microscale properties indicate a direct positive relationship between the two length scales, most notably in the relationship between nanoscale and microscale modulus. These findings indicate that diabetes-induced changes in material strength and modulus were driven by alterations at the nanoscale.
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    Nanoscale Morphology of Type I Collagen is Altered in the Brtl Mouse Model of Osteogenesis Imperfecta
    (2011-01) Wallace, Joseph M.; Orr, Bradford G.; Marini, Joan C; Banaszak Holl, Mark M
    Bone has a complex hierarchical structure that has evolved to serve structural and metabolic roles in the body. Due to the complexity of bone structure and the number of diseases which affect the ultrastructural constituents of bone, it is important to develop quantitative methods to assess bone nanoscale properties. Autosomal dominant Osteogenesis Imperfecta results predominantly from glycine substitutions (80%) and splice site mutations (20%) in the genes encoding the α1 or α2 chains of Type I collagen. Genotype-phenotype correlations using over 830 collagen mutations have revealed that lethal mutations are located in regions crucial for collagen-ligand binding in the matrix. However, few of these correlations have been extended to collagen structure in bone. Here, an atomic force microscopy-based approach was used to image and quantitatively analyze the Dperiodic spacing of Type I collagen fibrils in femora from heterozygous (Brtl/+) mice (α1(I)G349C), compared to wild type (WT) littermates. This disease system has a well-defined change in the col1α1 allele, leading to a well characterized alteration in collagen protein structure, which are directly related to altered Type I collagen nanoscale morphology, as measured by the Dperiodic spacing. In Brtl/+ bone, the D-periodic spacing shows significantly greater variability on average and along the length of the bone compared to WT, although the average spacing was unchanged. Brtl/+ bone also had a significant difference in the population distribution of collagen D-period spacings. These changes may be due to the mutant collagen structure, or to the heterogeneity of collagen monomers in the Brtl/+ matrix. These observations at the nanoscale level provide insight into the structural basis for changes present in bone composition, geometry and mechanical integrity in Brtl/+ bones. Further studies are necessary to link these morphological observations to nanoscale mechanical integrity.