scholarly journals Mechanisms of soft tissue and protein preservation in Tyrannosaurus rex

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Elizabeth M. Boatman ◽  
Mark B. Goodwin ◽  
Hoi-Ying N. Holman ◽  
Sirine Fakra ◽  
Wenxia Zheng ◽  
...  
Keyword(s):  
Soft Tissue ◽  
Type I Collagen ◽  
Type I ◽  
Structural Protein ◽  
Geological Time ◽  
Natural Conditions ◽  
Fenton Chemistry ◽  
X Ray ◽  
Ftir Studies ◽  
Protein Preservation

Abstract The idea that original soft tissue structures and the native structural proteins comprising them can persist across geological time is controversial, in part because rigorous and testable mechanisms that can occur under natural conditions, resulting in such preservation, have not been well defined. Here, we evaluate two non-enzymatic structural protein crosslinking mechanisms, Fenton chemistry and glycation, for their possible contribution to the preservation of blood vessel structures recovered from the cortical bone of a Tyrannosaurus rex (USNM 555000 [formerly, MOR 555]). We demonstrate the endogeneity of the fossil vessel tissues, as well as the presence of type I collagen in the outermost vessel layers, using imaging, diffraction, spectroscopy, and immunohistochemistry. Then, we use data derived from synchrotron FTIR studies of the T. rex vessels to analyse their crosslink character, with comparison against two non-enzymatic Fenton chemistry- and glycation-treated extant chicken samples. We also provide supporting X-ray microprobe analyses of the chemical state of these fossil tissues to support our conclusion that non-enzymatic crosslinking pathways likely contributed to stabilizing, and thus preserving, these T. rex vessels. Finally, we propose that these stabilizing crosslinks could play a crucial role in the preservation of other microvascular tissues in skeletal elements from the Mesozoic.

A new model for packing of type-I collagen molecules in the native fibril

1981 ◽  
Vol 1 (10) ◽  
pp. 801-810 ◽  
Author(s):  
Karl A. Piez ◽  
Benes L. Trus
Keyword(s):  
Type I Collagen ◽  
Hexagonal Lattice ◽  
Three Dimensional ◽  
Equatorial Region ◽  
Type I ◽  
X Ray Diffraction ◽  
X Ray ◽  
Left Handed ◽  
Crystal Model ◽  
Collagen Molecules

A specific fibril model is presented consisting of bundles of five-stranded microfibrils, which are usually disordered (except axially) but under lateral compression become ordered. The features are as follows (where D = 234 residues or 67 nm): (1) D-staggered collagen molecules 4.5 D long in the helical microfibril have a left-handed supercoil with a pitch of 400–700 residues, but microfibrils need not have helical symmetry. (2) Straight-tilted 0.5-D overlap regions on a near-hexagonal lattice contribute the discrete x-ray diffraction reflections arising from lateral order, while the gap regions remain disordered. (3) The overlap regions are equivalent, but are crystallographically distinguished by systematic displacements from the near-hexagonal lattice. (4) The unit cell is the same as in a recently proposed three-dimensional crystal model, and calculated intensities in the equatorial region of the x-ray diffraction pattern agree with observed values.

Sub‐ and Supramolecular X‐Ray Characterization of Engineered Tissues from Equine Tendon, Bovine Dermis, and Fish Skin Type‐I Collagen

2020 ◽  
Vol 20 (5) ◽  
pp. 2000017 ◽  
Author(s):  
Alberta Terzi ◽  
Nunzia Gallo ◽  
Simona Bettini ◽  
Teresa Sibillano ◽  
Davide Altamura ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Skin Type ◽  
Type I ◽  
Fish Skin ◽  
X Ray ◽  
Engineered Tissues

Archaeological Bone from Macro- to Nanoscale: Heat-Induced Modifications at Low Temperatures

2009 ◽  
Vol 8 ◽  
pp. 157-172 ◽  
Author(s):  
Céline Chadefaux ◽  
Ina Reiche
Keyword(s):  
Electron Microscopy ◽  
Low Temperatures ◽  
Type I Collagen ◽  
Bone Structure ◽  
Heating Temperature ◽  
Global Analysis ◽  
Type I ◽  
Scanning Calorimetry ◽  
Bone Material ◽  
X Ray

The present work focuses on the characterization of structural modifications in bone material induced by heating at low temperatures (90 - 250°C). This is of outmost importance when archaeological bone material is concerned. Changes occurring in the structure of the type I collagen and of the mineral-organic arrangement are especially investigated. This precise characterization required the combination of complementary analytical techniques: Differential Scanning Calorimetry (DSC) for global analysis of the collagen state of conservation, Scanning Electron Microscopy coupled with an Energy Dispersive X-Ray system (SEM-EDX), micro-Proton-Induced X-ray and Gamma-ray Emission (micro-PIXE/PIGE) for chemical analysis of the mineral fraction, Infrared microspectroscopy in attenuated total reflectance mode (micro-ATR-FT-IR) combined with curve-fitting for microscopic investigations and Transmission Electron Microscopy (TEM) on ultrathin sections to characterize the modifications in the mineral/organic interface at nanoscale. New criteria characterizing the effect of a thermal treatment at low temperatures on the bone structure from the macroscopic to the nanoscale were determined. There are namely a broadening of the Haversian canals, the inversion of the turns to -sheet ratio in the collagen structure determined by decomposition of the amide I IR band as well as a shift of amide II IR band position with the heating temperature to lower wavenumbers. At nanoscale, melting of the organic phase and clustering of hydroxyapatite (HAP) bone crystals can be observed. For comparison, unheated archaeological bones have been analyzed in order to test if the heat-induced modification can be distinguished from diagenetic alterations, generally dissolution-recrystallisation processes, in soils.

Heat Treatment Strengthens Human Dentin

2008 ◽  
Vol 87 (8) ◽  
pp. 762-766 ◽  
Author(s):  
M. Hayashi ◽  
E.V. Koychev ◽  
K. Okamura ◽  
A. Sugeta ◽  
C. Hongo ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Stress Intensity ◽  
Type I Collagen ◽  
Type I ◽  
Third Molars ◽  
X Ray Diffraction ◽  
Intensity Factors ◽  
X Ray ◽  
Human Dentin ◽  
Triple Helices

The flexural strength of Type I collagen, the major organic component of human dentin, increases with heat. We hypothesized that human dentin can be strengthened by heating, which may help prevent fracture of non-vital teeth after restoration. Beam-shaped dentin specimens were obtained from the crowns of human third molars. The dentinal tubular orientations were arranged to run parallel or perpendicular to loading surfaces. The flexural and microtensile strengths of dentin in the parallel specimens were 2- to 2.4-fold greater after being heated between 110°C and 140°C for 1 hr. The stress intensity factors at fracture also increased after specimens were heated. The x-ray diffraction analyses suggested that shrinking of the lateral packing of the collagen triple-helices from 14 Å to 11 Å was the probable cause of the strengthening of heated dentin. We conclude that heat treatment strengthens human dentin.

X-ray diffraction patterns and anatomical properties of claw tissues of beef and dairy cattle

2007 ◽  
Vol 145 (6) ◽  
pp. 623-633 ◽  
Author(s):  
M. P. BROWNE ◽  
D. W. L. HUKINS ◽  
J. M. S. SKAKLE ◽  
C. H. KNIGHT ◽  
K. A. K. HENDRY ◽  
...  
Keyword(s):  
Soft Tissue ◽  
Dairy Cattle ◽  
Type I ◽  
X Ray Diffraction ◽  
Dorsal Wall ◽  
X Ray ◽  
Dairy Heifers ◽  
Physical Measurements ◽  
Proximal Site ◽  
Diffraction Patterns

SUMMARYMedial claws from the right hind feet were obtained post mortem from four 19–20-month-old beef heifers and from four 28-month-old first-calving dairy heifers 3–4 days postpartum. X-ray diffraction (XRD) studies were undertaken on samples of soft and hard (cornified) integumental tissues of dorsal wall, sole and heel (bulb) for varying sites and planes of exposure. The measurements were interpreted as defining diffraction patterns and intermolecular spacings of cytoskeletal and extracellular fibrous structural proteins. The orientation of these proteins was examined in relation to physical characteristics and function including bearing of body weight by these tissues.Physical measurements taken included impression hardness which showed typically greater values for wall than sole and variable differences between horn of dairy and beef origin and husbandry systems. Claws from dairy heifers had significantly smaller values for toe (dorsal wall) angle, claw height and heel height and thickness of solear horn and heel soft tissue. Although few were studied, the results reflected typical husbandry origins and indicated the susceptibility to the lesion formation well recognized in postpartum dairy cattle.Typical XRD patterns for horn samples showed defined arcs of reflectance on the equatorial axis consistent with findings for the presence of α-helices in fibrils reported to occur in other hard-keratin-containing integumental tissues. However, reflectance on the meridional axis also reported for these other tissues was not detected. A similar defined pattern was obtained for less than 0·10 of samples of internal soft pre-cornified epidermal and attached dermal tissue although the values for intermolecular ‘d’ spacing for these were consistent with those reported for type I collagen. Diffuse reflection patterns were thus evident for the majority of samples of soft tissue epidermis and dermis and also for adipose tissue of the digital cushion.The formation of defined arcs of reflectance allowed the determination of fibril alignment in wall and solear horn. For the orientated samples of dorsal wall horn tissue, the outer layer showed a longitudinal angle of orientation essentially maintained proximal to distal. This pattern was maintained throughout the depth of horn at the proximal site. In contrast, layers in mid-wall and towards the distal edge showed a greater circumferential (horizontal) orientation in sections collected anterior to posterior towards the inner corial, including laminar, tissues. The orientation of fibrils in inner wall horn appears to relate to the direction of load-bearing forces in connecting horn to the distal phalanx. Horizontal alignment of fibrils was observed in the sole. In presenting the long axis of cells to the ground surface this orientation may facilitate erosive forces and contribute to the thinning of cornified sole horn under adverse underfoot conditions.

A MODEL OF TYPE I COLLAGEN FIBRILLOGENESIS BASED ON DIFFUSION LIMITED AGGREGATION

1995 ◽  
Vol 03 (04) ◽  
pp. 1033-1039
Author(s):  
JOHN PARKINSON ◽  
KARL E. KADLER ◽  
ANDY BRASS
Keyword(s):  
Type I Collagen ◽  
Unit Length ◽  
The Body ◽  
Biological Macromolecules ◽  
Type I ◽  
Structural Protein ◽  
Diffusion Limited Aggregation ◽  
Mass Unit ◽  
Diffusion Limited

The development of shape and form is intrinsic to the structure and function of many biological macromolecules including tubulin, actin and collagen. Type I collagen is a major structural protein in the body, providing mechanical strength for tissues such as bone and skin. It is present in the form of fibrils which display a regular banding pattern known as D-periodicity (where D = 67 nm). Type I collagen is a long rod-like molecule (300 nm ×1.5 nm) consisting of a triple helix formed from three polypeptide chains. In vivo and in vitro studies have shown that collagen molecules self-assemble in a regular D-staggered array to form striated fibrils. Further studies have shown that the process, termed fibrillogenesis, is entropy driven. A model based on diffusion limited aggregation was used to investigate the properties of rod self-assembly. This simple model reproduced several experimentally observed features of collagen fibril morphology including a linear mass/unit length profile and a preference for tip growth.

scholarly journals Synthesis of Organic-Inorganic Hybrid Material with a Synergistic Interface as a Release Agent for Free Acid β-Hydroxy-β-Methyl Butyrate

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Beatriz A. Andrade-Espinoza ◽  
Gregorio G. Carbajal-Arizaga ◽  
Selma Rivas-Fuentes ◽  
Karla Nuño ◽  
José Benito Pelayo-Vázquez ◽  
...  
Keyword(s):  
Hybrid System ◽  
Type I Collagen ◽  
Free Acid ◽  
Inorganic Compounds ◽  
Toxicity Tests ◽  
Type I ◽  
Scanning Electron Microscopy Data ◽  
Inorganic Hybrid ◽  
X Ray ◽  
Methyl Butyrate

We report the preparation and characterization of a new organic-inorganic hybrid system composed of type-I collagen and ZnAl layered double hydroxide (LDH) particles loaded with β-hydroxy-β-methyl butyrate (HMB) by coprecipitation reaction. X-ray diffraction (peaks well agree with those reported in the literature), infrared spectroscopy (stretching bonds for both organic-inorganic compounds), and X-ray photoelectron spectroscopy confirmed the hybrid system retained HMB in the carboxylate form, and a small fraction turned to the acid form. In both cases, the HMB molecules are assembled to the LDH surface. The hybrid compound results in improved thermal stability for HMB and collagen, as shown by thermal analysis. Scanning electron microscopy data reflects different arrangements from LDH sheets with interesting physicochemical properties since LDH and collagen protect free HMB and make it more bioavailable and functional. In vitro studies as part of high-throughput screening strategies indicated that LDH hybrids reduced cell viability around 75-90%, which is an acceptable viability value because of the L6 cell line susceptibility. However, all new nanomaterials must be carefully analyzed by different toxicity tests because a single test does not evaluate complete physiological compartments.

scholarly journals Mutations in type I collagen genes resulting in osteogenesis imperfecta in humans.

2002 ◽  
Vol 49 (2) ◽  
pp. 433-441 ◽  
Author(s):  
Anna Gajko-Galicka
Keyword(s):  
Osteogenesis Imperfecta ◽  
Bone Disease ◽  
Type I Collagen ◽  
Wide Spectrum ◽  
Dominant Negative ◽  
Structural Defects ◽  
Collagen Molecule ◽  
Type I ◽  
Structural Protein ◽  
Collagen Genes

Osteogenesis imperfecta (OI), commonly known as "brittle bone disease", is a dominant autosomal disorder characterized by bone fragility and abnormalities of connective tissue. Biochemical and molecular genetic studies have shown that the vast majority of affected individuals have mutations in either the COL1A1 or COL1A2 genes that encode the chains of type I procollagen. OI is associated with a wide spectrum of phenotypes varying from mild to severe and lethal conditions. The mild forms are usually caused by mutations which inactivate one allele of COL1A1 gene and result in a reduced amount of normal type I collagen, while the severe and lethal forms result from dominant negative mutations in COL1A1 or COL1A2 which produce structural defects in the collagen molecule. The most common mutations are substitutions of glycine residues, which are crucial to formation and function of the collagen triple helix, by larger amino acids. Although type I collagen is the major structural protein of both bone and skin, the mutations in type I collagen genes cause a bone disease. Some reports showed that the mutant collagen can be expressed differently in bone and in skin. Since most mutations identified in OI are dominant negative, the gene therapy requires a fundamentally different approach from that used for genetic-recessive disorders. The antisense therapy, by reducing the expression of mutant genes, is able to change a structural mutation into a null mutation, and thus convert severe forms of the disease into mild OI type I.

scholarly journals On the synthesis and characterization of β-tricalcium phosphate scaffolds coated with collagen or poly (D, L-lactic acid) for alveolar bone augmentation

2017 ◽  
Vol 11 (04) ◽  
pp. 496-502 ◽  
Author(s):  
Isadora S. Deschamps ◽  
Gabriel L. Magrin ◽  
Ricardo S. Magini ◽  
Márcio C. Fredel ◽  
Cesar A.M. Benfatti ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Tricalcium Phosphate ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Porous Ceramic ◽  
Polyurethane Foams ◽  
Type I ◽  
X Ray ◽  
Collagen Group ◽  
Coating Method

ABSTRACT Objectives: After tooth loss, dimensional alterations on the alveolar bone ridge can occur that can negatively affect the placement of dental implants. The purpose of this study was to evaluate the synthesis, and mechanical properties of β-tricalcium phosphate (β-TCP) scaffolds coated with bioabsorbable polymers, namely, collagen and poly (D, L-lactic acid) (PDLLA). Materials and Methods: β-TCP powder was obtained by reactive milling and then characterized by X-ray diffraction and scanning electron microscopy/energy dispersive X-ray spectroscopy (SEM/EDS). β-TCP scaffolds were obtained by replica method, in which polyurethane foams are immersed in β-TCP suspension and thereafter submitted to a thermal treatment to remove the polyurethane and sinter the ceramic. Type-I collagen or PDLLA were used to coat the β-TCP scaffolds by dip-coating method. Scaffolds were separated in four groups depending on the coating material: noncoated (Group A), double immersion in collagen (Group B), double immersion in PDLLA (Group C), and ten immersions in PDLLA (Group D). Samples were characterized by compressive tests and SEM/EDS. Data were statistically analyzed through two-way ANOVA (p = 0.05). Results: Chemical and microscopic analyses revealed proper morphology and chemical composition of powder particles and scaffolds with or without polymeric coatings. Scaffolds coated with PDLLA showed higher compressive strength (0.11 ± 0.054 MPa) than those of collagen (0.022 ± 0.012 MPa) or noncoated groups (0.024 ± 0.012 MPa). Conclusions: The coating method of β-TCP with PDLLA revealed a potential strategy to increase the mechanical strength of porous ceramic materials while collagen can enhance cell migration.

The Effects of Different Hydroxyapatite/TiO2 Composite Coatings on Protein Expression of Osteoblast

2009 ◽  
Vol 610-613 ◽  
pp. 1104-1108 ◽  
Author(s):  
Jian Ye Han ◽  
Zhen Tao Yu ◽  
Lian Zhou
Keyword(s):  
Protein Expression ◽  
Type I Collagen ◽  
Composite Coatings ◽  
Type I ◽  
X Ray Diffraction ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Compound Formation ◽  
X Ray ◽  
Polymerase Chain

Hydroxyapatite/TiO2 composite material was coated onto Ti25Nb3Mo2Sn3Zr (TLM) alloy substrate. To study the effects of hydroxyapatite/TiO2 composite coatings on bone-related protein expression, the osteoblast were cultured with composite coatings for different times. The phase transformation and compound formation of the HA/TiO2 coatings were investigated using XRD (X-ray diffraction). The mRNA expression of Type I collagen, alkaline phosphatase (ALP) and osteocalcin were studied by RT-PCR (reverse transcriptional polymerase chain reaction). The titania delayed the crystallization of HA. The mRNA expressions of Type I collagen are decreased as the increasing of TiO2 percentage. The mRNA expressions of osteocalcin are approached. The ALP expression on H4 coating (HA/TiO2 mol ration is 5) after the osteoblast cultured with composite coating for 6 days is the highest. The increasing of TiO2 amount decreases the bioactivity of the composite coatings.

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