The swelling of protein fibres. Part I. The swelling of collagen

Lloyd, Dorothy Jordan; Marriott, R. H.; Pleass, Winnifred Bertha

doi:10.1039/tf9332900554

Cited by 20 publications

(10 citation statements)

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“…The swelling has several consequences regarding the processing of collagen. The collagen molecules are separated and uncoupled from the stabilizing surrounding collagen molecules [135, 343, 344], and the material appears glassy and partly transparent. While soluble collagen is extracted, acidic pH creates a high internal tension of crosslinked collagen in tissue with a maximum of pH 3.…”

Section: Processing Collagenous Tissues—the Tools and Their Effectsmentioning

confidence: 99%

Processing of collagen based biomaterials and the resulting materials properties

2019

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Collagen, the most abundant extracellular matrix protein in animal kingdom belongs to a family of fibrous proteins, which transfer load in tissues and which provide a highly biocompatible environment for cells. This high biocompatibility makes collagen a perfect biomaterial for implantable medical products and scaffolds for in vitro testing systems. To manufacture collagen based solutions, porous sponges, membranes and threads for surgical and dental purposes or cell culture matrices, collagen rich tissues as skin and tendon of mammals are intensively processed by physical and chemical means. Other tissues such as pericardium and intestine are more gently decellularized while maintaining their complex collagenous architectures. Tissue processing technologies are organized as a series of steps, which are combined in different ways to manufacture structurally versatile materials with varying properties in strength, stability against temperature and enzymatic degradation and cellular response. Complex structures are achieved by combined technologies. Different drying techniques are performed with sterilisation steps and the preparation of porous structures simultaneously. Chemical crosslinking is combined with casting steps as spinning, moulding or additive manufacturing techniques. Important progress is expected by using collagen based bio-inks, which can be formed into 3D structures and combined with live cells. This review will give an overview of the technological principles of processing collagen rich tissues down to collagen hydrolysates and the methods to rebuild differently shaped products. The effects of the processing steps on the final materials properties are discussed especially with regard to the thermal and the physical properties and the susceptibility to enzymatic degradation. These properties are key features for biological and clinical application, handling and metabolization.

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Section: Processing Collagenous Tissues—the Tools and Their Effectsmentioning

confidence: 99%

Processing of collagen based biomaterials and the resulting materials properties

2019

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“…Interesting information can be obtained from experiments with gelatine gels containing an admixture of albumin. Instructions for preparing gelatine/albumin gel are given in the Appendix (p. 314).…”

Section: Cha Ptermentioning

confidence: 99%

Principles of biological microtechnique; a study of fixation and dyeing

Baker¹

1958

185

172

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The Reactions of Fixatives with Proteins, i. The Visible Effects 31 3 The Reactions of Fixatives with Proteins. 2. The Chemical Changes 4 The Reactions of Fixatives with Tissues and Cells: Methods of Research 5 Primary Fixatives Considered Separately, i . Coagulants 6 Primary Fixatives Considered Separately. 2. Noncoagulants III 7 Fixative Mixtures PART II: DYEING 8 Introduction to the Chemical Composition of Dyes 9 The Classification of Dyes 10 The Direct Attachment of Dyes to Tissues 1 1 The Indirect Attachment of Dyes to Tissues 12 The Differential Action of Dyes 13 Metachromasy 14 The Blood Dyes 15 '^e specially the latter's lactophenol. Amann called his fluids Beohachtiingsmedien, to indicate that they not only prevented the decay of tissues, but were media in which cells might remain during microscopical examination. It is desirable that research FIXATIONLiving cytoplasm commonly has a refractive index (r.i.) in the neighbourhood of 1-353;*^^'*^^t hat is to say, not very much higher than that of the saline solutions in which cells are commonly immersed for vital study. An aqueous solution of sodium chloride at 0*9% has an r.i. of i*335.^^-"-When cells are examined alive in such media, a w^ater-immersion objective w^ill give almost as good resolution as a first-rate oil-immersion objective, for the high numerical aperture of the latter will be partly wasted. One may surround living cells with innocuous media of the same r.i. as the cytoplasm ** and thus obtain slightly higher resolution (as well as gaining other advantages), but the difference will not be great. As soon, however, as a fixative acts, a profound change occurs. The evidence suggests ** that the protoplasm is now represented by interlacing sub-microscopic fibres having the r.i. of dry protein (about 1*54). These fibres lie in water, if the fixative is aqueous; this can be replaced by media of any desired refractive index. If a medium of r.i. close to that of dry protein is used (Canada balsam, for instance), two results ensue: almost perfect transparency is obtained (which may be modified as desired by the use of dyes), and oil-immersion objectives can be used at their full aperture. This fact should not, however, be too strongly stressed, for the making of a permanent microscopical preparation involves considerable shrinkage of the tissues of organisms (p. 76), and this reduces or nullifies the advantage of higher microscopical resolution. The advantage can be fully secured only if the object to be examined happens to be unshrinkable by the processes involved in making a permanent preparation. The valves of diatoms provide an example. Some of the constituent parts of organisms do not require fixation, because they are not subject to autolysis and are resistant to bacteria and moulds and to most of the reagents ordinarily used in microtechnique. Examples are chitin, cellulose, scleroproteins, certain inorganic crystals, and amorphous silica. Most such substances not only do not need fixation but are not acted upon by fixatives; or, if acted upo...

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“…The interaction between collagen and aqueous solutions has been studied for almost a century. However, the majority of research on this topic was focused on the interaction of aqueous solutions with soft tissue collagen (e.g., Jordan Lloyd et al, 1933;Bowes and Kenten, 1947;Zhang et al, 2000). In contrast, comparable data on the significantly more stable mineralized collagen are sparse (McKernan and Dailly, 1966;Lees, 1989;Pfretzschner, 2000;Fernández-Seara et al, 2002;Pfretzschner, 2006;Ni et al, 2007;Marinozzi et al, 2014).…”

Section: Influence Of the Chemical Environment On The Organic Phasementioning

confidence: 99%

Experimental Aqueous Alteration of Cortical Bone Microarchitecture Analyzed by Quantitative Micro-Computed Tomography

et al. 2021

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Bones are one of the most common vertebrate fossil remains and are widely used as proxy archives in palaeontology and archaeology. Previous histological analyses have shown that bone microarchitecture is mostly well-preserved in fossil remains, but partially or even entirely lost in most archaeological specimens. As a consequence, processes occurring during early diagenesis are pivotal for the preservation of bones and a better understanding of these processes would be required to assess the significance of information stored in fossilized bones. Although much of the changes occur at the nanometer scale, determining the resistance of bone microarchitecture to diagenetic alteration on a microscopic scale constitutes a prerequisite for more detailed studies. Here, results from the first comparative in vitro taphonomy study of cortical bone simulating conditions potentially encountered in early diagenetic settings are presented. In order to accelerate anticipated early diagenetic changes and to facilitate their study in a practical framework, cortical bone samples were exposed to aqueous solutions with temperature, time, and composition of the experimental solutions as controlled parameters. Before and after the experiments, all samples were characterized quantitatively using micro-computed tomography to document structural changes. The results show that the overall change in cortical porosity predominantly occurred in canals with diameters ≤9 µm (∆Ct.Po = ±30%). Furthermore, the data also show that the solution composition had a stronger impact on changes observed than either temperature or time. It was also found that samples from the two experimental series with a freshwater-like solution composition showed a characteristic reaction rim. However, it remains unclear at present if the observed changes have an impact on reactions occurring at the nanometer scale. Nonetheless, the results clearly demonstrate that on a micrometer scale down to 3 μm, bone microarchitecture is largely resistant to aqueous alteration, even under very different physicochemical conditions. In addition, the data illustrate the complexity of the interaction of different diagenetic factors. The results presented here provide a solid framework for future investigations on reaction and transport mechanisms occurring during the early diagenesis of fossil bones.

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The swelling of protein fibres. Part I. The swelling of collagen

Cited by 20 publications

References 0 publications

Processing of collagen based biomaterials and the resulting materials properties

Processing of collagen based biomaterials and the resulting materials properties

Principles of biological microtechnique; a study of fixation and dyeing

Experimental Aqueous Alteration of Cortical Bone Microarchitecture Analyzed by Quantitative Micro-Computed Tomography

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