Revisit the pre-transition of type I collagen denaturation in dilute solution by ultrasensitive differential scanning calorimetry

2012 ◽  
Vol 548 ◽  
pp. 1-5 ◽  
Author(s):  
Lirong He ◽  
Changdao Mu ◽  
Defu Li ◽  
Wei Lin
Keyword(s):  
Differential Scanning Calorimetry ◽  
Type I Collagen ◽  
Type I ◽  
Dilute Solution ◽  
Scanning Calorimetry ◽  
Collagen Denaturation

scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

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.

scholarly journals Mesenchymal Stem Cells Remodeling of Adsorbed Type I Collagen – Effect of Collagen Oxidation

2021 ◽  
Author(s):  
Regina Komsa Penkova ◽  
Galya Stavreva ◽  
Stanimir Kyurkchiev ◽  
Kalina Belemezova ◽  
Svetla Todinova ◽  
...  
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Structural Changes ◽  
Type I Collagen ◽  
Significant Inhibition ◽  
Type I ◽  
Scanning Calorimetry ◽  
Multiple Samples ◽  
Collagen Type 1

Abstract: The effect of collagen type 1 (Col I) oxidation on Adipose Tissue-Derived Mesenchymal Stem Cells (ADMSCs) remodeling is described as a model for acute oxidative stress. Morphologically, remodeling was presented by a mechanical rearrangement of adsorbed FITC-Col I and a trend for its organization in a fibril-like pattern - a process strongly abrogated in oxidized samples, but without visible changes in cell morphology. The cellular proteolytic activity was quantified in multiple samples utilizing fluorescence de-quenching (FRET effect). In the presence of ADMSCs a significant increase of native FITC-Col I fluorescence was observed, almost absent in the oxidized samples. Parallel studies in cell-free systems confirmed the enzymatic de-quenching of native FITC-Col I by Clostridial collagenase, again showing significant inhibition in oxidized samples. The structural changes in the oxidized Col I was further studied by Differential Scanning Calorimetry: an additional endotherm at 33.6°C along with the typical for native Col I at 40.5°C with sustained enthalpy (∆H) was observed in oxidized samples. Collectively, it has been evidenced that remodeling of Col I by ADMSCs is altered upon oxidation due to the intrinsic changes in the protein structure, thus presenting a novel mechanism for the control of stem cells' behavior toward collagen.

scholarly journals MOLECULAR CHARACTERISTICS OF ACID AND PEPSIN SOLUBLE COLLAGENS FROM THE SCALES OF GOLDEN CARP (PROBARBUS JULLIENI)

2017 ◽  
pp. 450 ◽  
Author(s):  
Ali Muhammed Moula Ali ◽  
Soottawat Benjakul ◽  
Hideki Kishimura
Keyword(s):  
Amino Acid ◽  
Type I Collagen ◽  
Helical Structure ◽  
Dry Weight ◽  
Total Amino Acid ◽  
Molecular Characteristics ◽  
Type I ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Golden Carp

Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were isolated from the scales of golden carp (Probarbus jullieni). Both ASC and PSC, identified as type I collagen, contained α- and β-chains as the dominant constituents. ASC and PSC had the yields of 0.42 and 1.16 g 100 g‒1 (dry weight basis), respectively. Amino acid composition revealed that glycine constituted 1/3 of total amino acid residues and no cysteine was found. ASC and PSC had imino acid contents of 197 and 202 residues/1000 residues, respectively. Fourier transform infrared spectroscopy (FTIR) and circular dichroism (CD) spectra indicated high integrity of the triple helical structure of both collagens. Based on differential scanning calorimetry (DSC), ASC and PSC had Tmax of 37.67 and 37.83 °C, respectively. Both collagens exhibited high solubility in acidic pH range (1‒3) and the decrease in solubility was found in the presence of NaCl at concentrations above 30 g L‒1. The overall results demonstrated that scales of golden carp could serve as another source of collagen.

scholarly journals Effects of grape seed extract on properties of type I collagen scaffolds

2020 ◽  
Vol 2 (2) ◽  
Author(s):  
Claudio Fernandes Garcia ◽  
Virginia C. A. Martins ◽  
Ana M. G. Plepis
Keyword(s):  
Type I Collagen ◽  
Crosslinking Agent ◽  
Grape Seed Extract ◽  
Grape Seed ◽  
Seed Extract ◽  
Type I ◽  
Scanning Calorimetry ◽  
Phosphate Buffered Saline ◽  
Collagen Suspension

 To obtain a material with potential for use in tissue engineering, anionic collagen was obtained from porcine serosa (S) and bovine tendon (T) by alkaline hydrolysis for 72h. Part of this collagen was mixed with water to obtain 4 % (weight/weight) collagen suspension and part was solubilized in acetic acid pH 3.5 to obtain 1.5% (w/w) gel. The suspensions were mixed with their respective gels (2:1) (suspension: gel) and grape seed extract, whose main product is proanthocyanidin, was added at concentrations of 0.03% and 0.5%, thus obtaining the scaffolds SC (serosa collagen suspension and gel), TC (tendon collagen suspension and gel), SCP003 (SC with 0.03% extract), TCP003 (TC with 0.03% extract), SCP05 (SC with 0.5% extract added) and TCP05 (TC with 0.5% extract). The materials were analyzed by differential scanning calorimetry (DSC), scanning electron microscopy (SEM) and characterized by phosphate buffered saline absorption assay and in vitro biological stability assay. By DSC it is observed that the addition of 0.5% of extract increases the denaturation temperature (Td) of collagen, indicating that at this concentration the extract acts as polymer crosslinking agent. SEM shows disorganized cross-section pores in all scaffolds, not exceeding 130 μm. Absorption and degradation assays indicated that the addition of 0.5% extract increases the absorption of phosphate buffered saline (PBS) by the scaffolds and decreases the degradation percentage by collagenase. These results suggests that the scaffolds can be used for different applications, e.g. as hemostatic agent.  

scholarly journals Extraction of Type I Collagen from Tilapia Scales Using Acetic Acid and Ultrafine Bubbles

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 288
Author(s):  
Junko Kuwahara
Keyword(s):  
Carbon Dioxide ◽  
Acetic Acid ◽  
Type I Collagen ◽  
Acetic Acid Solution ◽  
Type I ◽  
Collagen Concentration ◽  
Carbon Dioxide Gas ◽  
Collagen Denaturation ◽  
Sds Page ◽  
Medical Materials

Type I collagen is commonly used in medical materials and cosmetics. While it can be extracted from the skin and bones of mammals, marine collagen has attracted attention recently, since the use of mammalian collagen could result in zoonosis, and products containing mammalian collagen are avoided due to some religious beliefs. Chemical extractions using strong acids and alkalis, thermal extractions, and other nonconventional methods have been used for collagen extraction. However, there are few reports on environmentally friendly methods. Although heat extractions provide higher yields of collagen, they often cause collagen denaturation. Therefore, dilute acetic acid and ultrafine bubbles of oxygen, carbon dioxide, and ozone were used to extract type I collagen from tilapia scales. The extraction performance of the different conditions employed was qualitatively analyzed by SDS-PAGE electrophoresis, and the collagen concentration was quantified using circular dichroism spectroscopy by monitoring the peak intensity at 221 nm, which is specific to the triple helix of type I collagen. Collagen was extracted from tilapia scales with a yield of 1.58% by the aeration of ultrafine bubbles of carbon dioxide gas in a 0.1 M acetic acid solution for 5 h.

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