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Emerging Applications of X-ray Scattering in Controlling Structural Functions of Biomaterials

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Materials Chemistry".

Deadline for manuscript submissions: closed (1 November 2021) | Viewed by 4774

Special Issue Editors


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Guest Editor
School of Food Science and Nutrition, University of Leeds, Leeds, UK
Interests: nanoscience; physical chemistry; lipid biophysics; biomimetic self-assembly; X-ray scattering
Special Issues, Collections and Topics in MDPI journals

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Assistant Guest Editor
School of Health and Life Sciences, University of Teesside, Middleborough, UK
Interests: food colloids; food powders; biopolymers; microencapsulation

Special Issue Information

Dear Colleagues,

The emerging technologies in X-ray metrology have led to the most recent advances to reveal detailed structural information about biomaterials. This information directly feeds the development of new strategies and formulations of materials to address grand challenges in food, healthcare, and biomedical domains. The term “structural-functions” recognizes those particular functional properties which are directly or indirectly associated with structural features such as size, shape, assembly, hierarchy, and order/disorder properties. Generally speaking, the functions may address a particular application (e.g., theranostics, controlled release, etc.), or any kinds of interactions and kinetics of materials within a specific medium (e.g., fluidity, stability, aggregation).

Contributions to this Issue, in the form of original research or review articles, may cover all aspects of developments on understanding structural functions of different materials by small- and wide-angle X-ray scattering. Studies with multidisciplinary input, offering new methodologies or insights, are particularly welcome. Examples may include but are not limited to the design strategy and application-led understanding of semicrystalline polymers, lipid self-assemblies, inorganic and polymeric nanoparticles, biomineralization, porous systems, and 2D materials.

Dr. Amin Sadeghpour
Dr. Amin Farshchi
Guest Editors

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Structure–function correlations
  • X-ray scattering
  • Nanomaterials
  • (Semi)crystalline systems
  • Structural dynamics

Published Papers (2 papers)

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Research

12 pages, 3584 KiB  
Article
Short-Chain Mono-Alkyl β-D-Glucoside Crystals—Do They Form a Cubic Crystal Structure?
by Shigesaburo Ogawa and Isao Takahashi
Molecules 2022, 27(14), 4359; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27144359 - 07 Jul 2022
Cited by 1 | Viewed by 1291
Abstract
Three-dimensional liquid crystal (LC) phases, cubic LC phases, have been extensively studied as fascinating molecular assembled systems formed by amphiphilic compounds. However, similar structures have only been seen in rare instances in lipid crystal states in glycolipid crystal studies. In this study, we [...] Read more.
Three-dimensional liquid crystal (LC) phases, cubic LC phases, have been extensively studied as fascinating molecular assembled systems formed by amphiphilic compounds. However, similar structures have only been seen in rare instances in lipid crystal states in glycolipid crystal studies. In this study, we prepared short-chain n-alkyl β-D-glucosides (CnG) with an alkyl chain length n ranging from 4 to 6 and investigated their crystal structures. First, differential thermal analysis (DTA) and thermogravimetric analysis (TG) measurements showed the formation of hydrated crystals for C4G and C5G, respectively. Second, the crystal structures of CnG (n = 4, 5, 6) in both anhydrous and hydrated states were examined using a temperature-controlled powder X-ray diffraction (PXRD) measurement. Both hydrate and anhydrous crystals of C4G and C5G with critical packing parameters (CPPs) less than 0.33 formed cubic crystal phases. Bilayer lengths, calculated from the main diffraction peaks in each PXRD profile, depended on crystalline moisture for C5G, but no significant change was confirmed for C4G, indicating that the properties of each hydrophilic layer differ. However, C6G with a CPP of 0.42 formed a crystal structure with a modulated lamellar structure similar to C7G and C8G with similar CPP values. Thus, a glycolipid motif concept with a cubic crystal structure was demonstrated. Full article
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18 pages, 11473 KiB  
Article
Dependence of the Nanoscale Composite Morphology of Fe3O4 Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study
by Martin A. Schroer, Po-Sheng Hu, Natalia Tomasovicova, Marianna Batkova, Katarina Zakutanska, Po-Yi Wu and Peter Kopcansky
Molecules 2021, 26(16), 4864; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26164864 - 11 Aug 2021
Cited by 2 | Viewed by 2401
Abstract
Understanding the formation process and the spatial distribution of nanoparticle (NP) clusters on amyloid fibrils is an essential step for the development of NP-based methods to inhibit aggregation of amyloidal proteins or reverse the assembling trend of the proto-fibrillary complexes that prompts pathogenesis [...] Read more.
Understanding the formation process and the spatial distribution of nanoparticle (NP) clusters on amyloid fibrils is an essential step for the development of NP-based methods to inhibit aggregation of amyloidal proteins or reverse the assembling trend of the proto-fibrillary complexes that prompts pathogenesis of neuro degeneration. For this, a detailed structural determination of the diverse hybrid assemblies that are forming is needed, which can be achieved by advanced X-ray scattering techniques. Using a combined solution small angle X-ray scattering (SAXS) and atomic force microscopy (AFM) approach, this study investigates the intrinsic trends of the interaction between lysozyme amyloid fibrils (LAFs) and Fe3O4 NPs before and after fibrillization at nanometer resolution. AFM images reveal that the number of NP clusters interacting with the lysozyme fibers does not increase significantly with NP volume concentration, suggesting a saturation in NP aggregation on the fibrillary surface. The data indicate that the number of non-adsorbed Fe3O4 NPs is highly dependent on the timing of NP infusion within the synthesis process. SAXS data yield access to the spatial distribution, aggregation manner and density of NP clusters on the fibrillary surfaces. Employing modern data analysis approaches, the shape and internal structural morphology of the so formed nanocomposites are revealed. The combined experimental approach suggests that while Fe3O4 NPs infusion does not prevent the fibril-formation, the variation of NP concentration and size at different stages of the fibrillization process can impose a pronounced impact on the superficial and internal structural morphologies of these nanocomposites. These findings may be applicable in devising advanced therapeutic treatments for neurodegenerative diseases and designing novel bio-inorganic magnetic devices. Our results further demonstrate that modern X-ray methods give access to the structure of—and insight into the formation process of—biological–inorganic hybrid structures in solution. Full article
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