scholarly journals Study of the Maturation of the Organic (Type I Collagen) and Mineral (Nonstoichiometric Apatite) Constituents of a Calcified Tissue (Dentin) as a Function of Location: A Fourier Transform Infrared Microspectroscopic Investigation

2001 ◽  
Vol 16 (4) ◽  
pp. 750-757 ◽  
Author(s):  
David Magne ◽  
Pierre Weiss ◽  
Jean-Michel Bouler ◽  
Olivier Laboux ◽  
Guy Daculsi
Keyword(s):  
Fourier Transform ◽  
Type I Collagen ◽  
Fourier Transform Infrared ◽  
Type I ◽  
Calcified Tissue

scholarly journals Fourier transform infrared conformational investigation of type I collagen aged by in vitro induced dehydration and non-enzymatic glycation treatments

2017 ◽  
Vol 90 (1) ◽  
Author(s):  
Maria Grazia Bridelli ◽  
Chiaramaria Stani ◽  
Roberta Bedotti
Keyword(s):  
Fourier Transform ◽  
Protein Structure ◽  
Conformational Changes ◽  
Self Assembly ◽  
Type I Collagen ◽  
Protein Secondary Structure ◽  
Fourier Transform Infrared ◽  
Type I ◽  
Absorption Bands

The two main ageing-inducing events in the collagenous tissues are the water loss and the formation of intermolecular crosslinks based on the reaction of collagen with matrix carbohydrates, following a mechanism known as non-enzymatic-glycation. With the aim to mimic the two deleterious processes for the protein structure, rat-tail collagen was submitted to hydration changes and allowed to interact with two sugars characterized by different reducing properties, D-glucose and D-ribose. Fourier transform infrared (FTIR) spectroscopy was employed to investigate the conformational changes induced in the protein by the two treatments by analyzing the subsequent spectra modifications. FTIR spectra monitored: i) the amplitude and position changes of the two characteristic absorption bands OH stretching and Amide I, in dependence on the humidity level: a significant hysteresis effect in the ν(OH) band (ν~3400 cm–1) amplitude of the protein dehydrated and then rehydrated to the initial relative humidity (aw=0.92- 0.06) may be related to the enhancement of the β-sheet fraction in the protein structure as revealed by the parallel modification in the Amide I band (ν~1650 cm–1); ii) the area of the carbohydrate double band peaking at 1080 cm–1 and 1031 cm–1, associated to the accumulation of the glycation products, depending on the sugar concentration and incubation time. The association of both sugars to collagen only minimally affects the protein secondary structure as revealed by Amide I band Gaussian analysis. The whole set of results suggests hints to hypothesize a self-assembly model for collagen molecules induced by ageing.

Structural Differences between Type I and Type IV Collagen in Biological Tissues Studied in vivo by Attenuated Total Reflection/Fourier Transform Infrared Spectroscopy

1992 ◽  
Vol 46 (4) ◽  
pp. 626-630 ◽  
Author(s):  
Yukihiro Ozaki ◽  
Aritake Mizuno ◽  
Fumiko Kaneuchi
Keyword(s):  
Fourier Transform ◽  
Type Iv Collagen ◽  
Type I Collagen ◽  
Fourier Transform Infrared ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Random Coil ◽  
Type I ◽  
Type Iv ◽  
Helix Formation

Attenuated total reflection/Fourier transform infrared (ATR/FT-IR) spectra have been obtained in a nondestructive manner for the anterior surface, interior part, and posterior surface of the sclera, for the epithelium, Bowman's membrane, stroma, and endothelium of the cornea, and for the inner section of the Achilles' tendon of a rabbit. The corresponding spectra have been remeasured for the rabbit anterior and posterior lens capsule for purposes of comparison. The spectra of the three parts of the sclera and of the Bowman's membrane and stroma of the cornea are very close to the spectrum of purified type I collagen, confirming that their major components are type I collagen. The spectrum of the tendon is also very similar to that of purified type I collagen, but it contains a small contribution from hyaluronic acid in the 1100-1000 cm−1 region. The amide I bands of the type I collagen-containing tissues are sharp and symmetrical, and their frequencies (1642 cm−1) are almost identical to that (1640 cm−1) of polyglycine II, which takes a 3, helix formation, indicating that the secondary structure of type I collagen in the tissues examined is for practical purposes a slightly modified 31 helix. A comparison of the spectra of the type I collagen-containing tissues and those of the type IV collagen-containing tissues reveals that there are two major differences between them; one is the spectral features in the 1100-1000 cm1 region, where C-O stretching modes of polysaccharide are observed, and the other is the shape and frequency of the amide I band. Besides the peak at 1637 cm−1, the amide I bands of the type IV collagen-containing tissues have shoulders near 1650 and 1655 cm−1. This observation indicates that type IV collagen in the tissues examined assumes primarily a slightly modified 31 helix formation, but the percentages of α-helix and random coil structures are not negligible.

Coprecipitation of Cell Adhesion Molecule with Calcium Phosphate on Hydroxyapatite Ceramic

2006 ◽  
Vol 309-311 ◽  
pp. 767-770 ◽  
Author(s):  
Yu Sogo ◽  
Yuusuke Ishikawa ◽  
Nao Kondo ◽  
Eiji Uchimura ◽  
Ayako Oyane ◽  
...  
Keyword(s):  
Calcium Phosphate ◽  
Cell Adhesion Molecule ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Composite Layer ◽  
Phosphate Solution ◽  
Type I ◽  
Hydroxyapatite Ceramic ◽  
Tooth Roots ◽  
Calcified Tissue

Fibronectin (FN) and type I collagen (Col), which are kinds of extracelluar matrices, were coprecipitated with calcium phosphate to form a composite layer on a hydroxyapatite (HAP) ceramic using a supersaturated calcium phosphate solution (CP solution). The amounts of protein immobilized in the layers were determined to be 20.97±3.04 µg·cm-2 for FN, 5.26±0.19 µg·cm-2 for Col and 21.72±2.30 µg·cm-2 for simultaneously immobilized FN and Col. When osteoblastic MC3T3-E1 cells were cultured on the HAP ceramics with the composite layer containing FN and/or Col, calcified tissue was formed through the activity of the cells. The result showed that the composite layer accelerated the differentiation of MC3T3-E1 to bone-forming cells. It is assumed that osteoblastic cells in alveolar bone migrated and differentiated on the surface of the tooth roots when the artificial tooth roots were covered with the composite layer.

scholarly journals Isolation of papain-soluble collagen from the skin of snake-head fish (Channa striata)

2020 ◽  
pp. 87-93
Author(s):  
Andi Rahmayanti Ramli ◽  
Andi Rezky Annisa ◽  
Nur Alim Bahmid ◽  
Muhammad Dalvi Mustafa
Keyword(s):  
Fourier Transform ◽  
Moisture Content ◽  
Polyacrylamide Gel Electrophoresis ◽  
Fourier Transform Infrared ◽  
Helical Structure ◽  
Collagen Type I ◽  
Type I ◽  
Fish Skin ◽  
Soluble Collagen ◽  
Channa Striata

Snake-head fish (Channa striata) skin categorized a byproduct contains a higher concentration of collagen. The collagen can be extracted by using protease, which is known as Papain Soluble Collagen (PaSC). This study aimed to isolate the collagen from the snake-head fish skin using papain. The yield percentage and moisture content of PaSC in the skin was determined. Measurements using SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR) were performed to characterize the PaSC and its functional groups. The results showed that the yields and moisture content of PaSC were 8.9% and 6.07%, respectively. The PaSC characterized by two α-chains appeared as collagen type I. Fourier transform infrared (FTIR) spectra of PaSC confirmed a triple-helical structure of collagen. The results indicated that snake-head fish skin could be used as potential resources of collagen and papain can be used as an alternative affordable enzyme.

Microwave-assisted synthesis and evaluation of type 1 collagen–apatite composites for dental tissue regeneration

2018 ◽  
Vol 33 (1) ◽  
pp. 103-115 ◽  
Author(s):  
Kanwal Ilyas ◽  
Saba W Qureshi ◽  
Sadia Afzal ◽  
Roquyya Gul ◽  
Muhammad Yar ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Fourier Transform Infrared Spectroscopy ◽  
Sodium Dodecyl ◽  
Fourier Transform Infrared ◽  
Type I ◽  
Formation Behavior ◽  
Scanning Electron

The aim was to develop an economical and biocompatible collagen-based bioactive composite for tooth regeneration. Acid-soluble collagen was extracted and purified from fish scales. The design was innovated to molecularly tailor the surface charge sites of the nano-apatite providing chemical bonds with the collagen matrix via microwave irradiation technique. The obtained collagen was identified by sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis. The composites were characterized by Fourier transform infrared spectroscopy, thermogravimetric analysis/differential scanning calorimetry, and scanning electron microscopy. MC3T3-E1 cell lines were used to assess the biological effects of these materials by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-tetra zolium bromide (MTT) assay. Indirect contact test was performed by extracting representative elutes in cell culture media and sulforhodamine B analysis was performed. Chorioallantoic membrane assay was conducted to define the new vessels formation behavior. The purity of collagen extracts was determined and showed two α-chains, i.e. the characteristic of type I collagen. Fourier transform infrared spectroscopy showed the characteristic peaks for amide I, I, III, and phosphate for collagen and composites. Scanning electron microscopy images showed three-dimensional mesh of collagen/apatite nano-fibers. Nontoxic behavior of composites was observed and there were graded and dose-related effects on experimental compounds. The angiogenesis and vessels formation behavior were observed in bioactive collagen composite. The obtained composites have potential to be used for tooth structure regeneration.

Microstructure, Spectroscopic Studies and Nanomechanical Properties of Human Cortical Bone with Osteogenesis Imperfecta

2014 ◽  
Vol 1621 ◽  
pp. 163-168
Author(s):  
Chunju Gu ◽  
Dinesh R. Katti ◽  
Kalpana S. Katti
Keyword(s):  
Fourier Transform ◽  
Osteogenesis Imperfecta ◽  
Cortical Bone ◽  
Type I Collagen ◽  
Experimental Studies ◽  
Spectroscopic Studies ◽  
Type I ◽  
Healthy Human ◽  
Electron Microscopies ◽  
Human Cortical Bone

ABSTRACTBone is a natural protein (collagen)-mineral (hydroxyapatite) nanocomposite with hierarchically organized structure. Our previous work has demonstrated orientational differences in stoichiometry of hydroxyapatite resulting from orientationally dependent collagen-mineral interactions in bone. The nature of these interactions has been investigated both through molecular dynamics simulations as well as nanomechanical and infrared spectroscopic experiments. In this study, we report experimental studies on human cortical bone with osteogenesis imperfecta (OI), a disease characterized by fragility of bones and other tissues rich in type I collagen. About 90% of OI cases result from causative variant in one of the two structural genes (COL1A1 or COL1A2) for type I procollagens. OI provides an interesting platform for investigating how alterations of collagen at the molecular level cause changes in structure and mechanics of bone. Fourier transform spectroscopy, electron microscopy (SEM), and nanomechanical experiments describe the structural and molecular differences in bone ultrastructure due to presence of diseases. Photoacoustic-Fourier transform infrared spectroscopy (PA-FTIR) experiments have been conducted to investigate the orientational differences in molecular structure of OI bone, which is also compared with that of healthy human cortical bone. Further, in situ SEM static nanomechanical testing is conducted in the transverse and longitudinal directions in the OI bone. Microstructural defects and abnormities of OI bone were ascertained using scanning electron microscopies. These results provide an insight into molecular basis of deformation and mechanical behavior of healthy human bone and OI bone.

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