Natural Fibrous Proteins: Structural Analysis, Assembly, and Applications

Raaij, Mark J. van; Mitraki, Anna

doi:10.1002/9781118523063.ch11

Cited by 2 publications

(2 citation statements)

References 108 publications

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“…Collagen consists of rigid rod like triple helices with crosslinks that bind them into fibrils. Water can penetrate between the helices and expand the fibrils [ 27 ]. Hydroxyapatite precipitates around the fibrils [ 28 ] stabilizing the collagen against excessive water sorption induced expansion and attack by enzymes.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Dentine to Assess Bond Strength of Dental Composites

et al. 2015

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This study was performed to develop alternating dentine adhesion models that could help in the evaluation of a self-bonding dental composite. For this purpose dentine from human and ivory was characterized chemically and microscopically before and after acid etching using Raman and SEM. Mechanical properties of dentine were determined using 3 point bend test. Composite bonding to dentine, with and without use of acid pre-treatment and/or the adhesive, were assessed using a shear bond test. Furthermore, micro gap formation after restoration of 3 mm diameter cavities in dentine was assessed by SEM. Initial hydroxyapatite level in ivory was half that in human dentine. Surface hydroxyapatites decreased by approximately half with every 23 s of acid etch. The human dentine strength (56 MPa) was approximately double that of ivory, while the modulus was almost comparable to that of ivory. With adhesive use, average shear bond strengths were 30 and 26 MPa with and without acid etching. With no adhesive, average bond strength was 6 MPa for conventional composites. This, however, increased to 14 MPa with a commercial flowable “self–bonding” composite or upon addition of low levels of an acidic monomer to the experimental composite. The acidic monomer additionally reduced micro-gap formation with the experimental composite. Improved bonding and mechanical properties should reduce composite failures due to recurrent caries or fracture respectively.

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Section: Resultsmentioning

confidence: 99%

Characterization of Dentine to Assess Bond Strength of Dental Composites

et al. 2015

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“…In the case of fibrils, they are classified as non-amyloid and amyloids. Representative non-amyloid fibrillar structures are mainly related to motility and scaffold functions in the cell, such as actin fibrils, microtubules, collagen, among others [ 32 ]. On the other hand, amyloid fibrils are well known to be a hallmark of neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and type II diabetes, among other pathologies [ 3 ].…”

Section: Setting the Frame And Initial Considerationsmentioning

confidence: 99%

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

2020

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The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson’s disease and Alzheimer’s disease, among other aggregopathies. As a consequence, significant research efforts are directed towards the understanding of this process. In this review, we are focused on the use of UV-Visible Absorption Spectroscopy, Fluorescence Spectroscopy and Circular Dichroism to evaluate the self-organization of proteins and peptides in solution. These spectroscopic techniques are commonly available in most chemistry and biochemistry research laboratories, and together they are a powerful approach for initial as well as routine evaluation of protein and peptide self-assembly and aggregation under different environmental stimulus. Furthermore, these spectroscopic techniques are even suitable for studying complex systems like those in the food industry or pharmaceutical formulations, providing an overall idea of the folding, self-assembly, and aggregation processes, which is challenging to obtain with high-resolution methods. Here, we compiled and discussed selected examples, together with our results and those that helped us better to understand the process of protein and peptide aggregation. We put particular emphasis on the basic description of the methods as well as on the experimental considerations needed to obtain meaningful information, to help those who are just getting into this exciting area of research. Moreover, this review is particularly useful to those out of the field who would like to improve reproducibility in their cellular and biomedical experiments, especially while working with peptide and protein systems as an external stimulus. Our final aim is to show the power of these low-resolution techniques to improve our understanding of the self-assembly of peptides and proteins and translate this fundamental knowledge in biomedical research or food applications.

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Natural Fibrous Proteins: Structural Analysis, Assembly, and Applications

Cited by 2 publications

References 108 publications

Characterization of Dentine to Assess Bond Strength of Dental Composites

Characterization of Dentine to Assess Bond Strength of Dental Composites

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

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