Thermal behavior of in vitro mineralized anionic collagen matrices

In the present study porcine skin and bovine pericardium were used as a source of type I collagen. Both were submitted to an alkaline treatment and mineralized by the alternate soaking method. Thermal stability and extent of mineralization have been investigated using DSC and TG. After alkaline hydrolysis there is a decrease in thermal stability but mineralization stabilizes collagen structure. Thermogravimetric data have shown that the amount of hydroxyapatite present in bovine pericardium matrix (45%) was greater than on porcine skin matrix (20%). Presence of hydroxyapatite was confirmed by EDX.     

On the Effects of UV‐C and pH on the Mechanical Behavior,Molecular Conformation and Cell Viability of Collagen‐Based Scaffold for Vascular Tissue Engineering

Collagen‐based vascular substitutes represent in VTE a valid alternative for the replacement of diseased small‐calibre blood vessels. In this study, collagen gel‐based scaffolds were crosslinked combining modulation of pH and UV‐C radiation. The effects on the mechanical properties, on the molecular structure and on cell viability and morphology were investigated. The mechanical response increased as a function of pH or UV‐C dose and strongly depended on the test speed. Collagen molecular conformation resulted only slightly modified. While cell adhesion was not significantly altered, cell proliferation partially decreased in function of pH and UV‐C. These findings suggest that UV‐C treated collagen gels can represent an adequate substrate for VTE applications.

     

鲤鱼胶原蛋白的过敏原性研究

以鲤鱼鱼皮为研究对象,通过碱溶、酸溶、NaCl盐析等方法从鱼皮中分离纯化得到了胶原蛋白.SDS-PAGE分析显示,鲤鱼胶原蛋白由分子质量约为120 ku和115 ku的2条α链（α1与α2）、分子质量约为250 ku的β链以及大分子质量的γ链组成.分析比较鲤鱼胶原蛋白与鲢鱼小清蛋白的基本性质,结果显示：2种蛋白质的pH...     

猪皮胶原肽-锌螯合物的制备工艺研究

研究猪皮胶原肽-锌螯合物的制备工艺。以猪皮为原料，制备猪皮胶原肽-锌螯合物；以螯合率为指标，研究了猪皮胶原肽与锌质量比、pH、温度、时间对螯合率的影响；通过单因素试验、响应面法试验考察优化猪皮胶原肽的富锌工艺。结果显示，猪皮肽-锌螯合的最佳工艺为猪皮肽与锌质量比2:1，螯合pH 7.0，螯合温度50 ℃，螯合时间50 min，在此条件下，试验螯合率最佳，为69.27%，与模型预测值69.92%相近。该研究为新型生物肽 锌螯合物的研制、猪皮的高值化利用提供了依据。     

PEG‐dialdehyde–the new cross‐linking agent for collagen/elastin hydrogels

Collagen and elastin are the major proteins of an extracellular matrix. They possess attractive, complementary mechanical properties in their native state, but during isolation, its unique structure is destroyed, which affects the parameters of the materials. However, they still have excellent biological properties. The cross‐linking process improves the physicochemical properties of protein materials. The ideal cross‐linking agent should be effective and does not impair the biological properties of the material. Therefore, poly(ethylene) glycol‐dialdehyde was used in the study. The results show that the addition of poly(ethylene) glycol‐dialdehyde in combination with the neutralization of a collagen/elastin solution is a useful method for preparation of protein hydrogels. The gels are transparent and relatively stiff. They exhibit good mechanical properties, surface properties and are attractive for 3 T3 cells. Copyright © 2016 John Wiley & Sons, Ltd.     

The review of versatile application of collagen

This review reports recent advances in the versatile application of collagen. Collagen materials have attracted great attention because they exhibit properties required in cosmetic preparations, in the biomedical field, and in the tanning industry leading to leather production. Herein, the structure and application of collagen are discussed in general, and detailed examples are also drawn from scientific literature and practical work. Copyright © 2016 John Wiley & Sons, Ltd.     

胶原纤维为模版制备TiO2及La/TiO2纳米纤维及光催化活性研究

以胶原纤维为模版分别负载钛(Ti4+)或钛(Ti4+)和镧(La3+),在高温下煅烧制得TiO2和La/TiO2纳米纤维。通过扫描电镜(SEM)、场发射扫描电镜(FESEM)、X-射线衍射(XRD)、比表面积和孔径分析、X-射线光电子能谱(XPS)、紫外可见光谱(UV-Vis)等对这2种纳米纤维的结构和物理性能进行了表征。结果表明,TiO2和La/TiO2较完整地保持了胶原纤维的纤维状结构。在600~800℃范围内随着煅烧温度的升高,TiO2和La/TiO2的晶粒尺寸逐渐增大,晶格常数发生各相异性的变化。La/TiO2的相变温度在700~800℃之间,明显高于未掺杂TiO2的相变温度。N2吸附-脱附等温线按Langmiur分类为Ⅳ类,表明TiO2和La/TiO2纳米纤维具有介孔结构。与Degussa P25相比,TiO2和La/TiO2吸收光谱范围明显红移。当以可见光为光源进行酸性橙Ⅱ光助催化降解反应时,TiO2和La/TiO2纳米纤维均表现出比Degussa P25更高的催化活性。     

Effect of Temperature on Self‐Interaction of Human‐Like Collagen

Effects of temperature on self‐interaction of human‐like collagen (HLC) were investigated by hydrophobic interaction chromatography, calorimetric measurement, and sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE) analysis. Results show that three types of interaction roles may exist between HLC molecules at 3–50°C, which were divided into three narrower temperature ranges. In temperature range from 3–22°C, hydrogen bonding plays a key role in the formation of a gelatinous aggregate. In the range of 22–38°C, hydrophobic bonds accompanied by hydrogen bonds are involved in the formation compact aggregates. When temperature is above 38°C the hydrophobic effect formed in the HLC monomer results in the loss of its ability to self‐interact.     

Emulsion electrospinning of a collagen-like protein/PLGA fibrous scaffold: empirical modeling and preliminary release assessment of encapsulated protein

The effectiveness of a multifunctional scaffold produced by the electrospinning of emulsions composed of organic PLGA and aqueous collagen-like protein (denoted as Fol-8Col) solutions is demonstrated. The resultant Fol-8Col/PLGA fibrous scaffolds with homogeneous morphology have mean fiber diameters from 600 to 2,000 nm. A uniform distribution of encapsulated Fol-8Col in the fibers is observed by fluorescence microscopy. TEM is used to clarify the representative core/sheath structure of emulsion electrospun Fol-8Col/PLGA fibers. Preliminary release assessment of encapsulated Fol-8Col shows results of sustained release for more than one month from the Fol-8Col/PLGA fibrous mats. The cytocompatibility of fibroblast cell line L929 with the fibrous composite seems promosing.