Special Issue "Proteins and Biomineralisation"

A special issue of Crystals (ISSN 2073-4352). This special issue belongs to the section "Biomolecular Crystals".

Deadline for manuscript submissions: closed (10 August 2020).

Special Issue Editors

Dr. Teresa Roncal-Herrero
Website
Guest Editor
University of Leeds, Leeds, United Kingdom
Interests: soft mater characterisation; crystallisation; electron microscopy
Dr. Ashit Rao
Website
Guest Editor
Faculty of Science and Technology, University of Twente, Enschede, The Netherlands
Interests: biomineralisation, chemical biology; crystallisation; material chemistry

Special Issue Information

Dear Colleagues,

Exhibiting fascinating structure–property relations, biominerals have attracted enormous research interest as evolutionarily optimised materials with specialised functions. Several disciplines have contributed to the field of biomineralisation with primary motivations as (1) elucidating the formation and structure–property relationships of biomaterials and (2) emulating evolutionarily optimised material organisations by synthetic strategies. These endeavours, also stimulated by advances in high-resolution analytical techniques, have provided some fundamental understanding of biomineralisation.

Addressing the mechanisms and pathways of biomineralisation is a challenging task due to the minute length scales at which nucleation and growth phenomena take place as well as the dynamic nature of inorganic as well as organic precursors. This Special Issue aims to cover studies addressing the pathways and products of mineralisation regulated by biomolecules in biological and synthetic environments. In view of the different levels of protein structure ranging from amino acid sequence to aggregate states, we encourage contributions related to mineralisation controlled by complex biological and synthetic macromolecules. Potential topics include but are not limited to:

  • Crystal morphology, composition and polymorph guided by organic molecules;
  • Micro- and ultrastructure of natural or biomimetic composites;
  • Structural dynamics and self-association of molecules in mineralising environments;
  • Catalytic and structural functions of biomolecules in mineralisation;
  • Sequence, structure and post-translational modifications of proteins;
  • Protein-inspired control over nucleation and crystallisation;
  • Biomimetic processes and materials.

Submissions on novel developments, techniques, applications and review papers are all welcome.

Dr. Teresa Roncal-Herrero
Dr. Ashit Rao
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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. Crystals is an international peer-reviewed open access monthly 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 1600 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

  • Biomineralisation
  • Bio-inorganic interfaces
  • Composite materials
  • Crystal growth
  • Crystallisation pathways
  • Proteins
  • Macromolecules
  • Structure–property relations

Published Papers (3 papers)

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Research

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Open AccessArticle
Polycarboxylated Eggshell Membrane Scaffold as Template for Calcium Carbonate Mineralization
Crystals 2020, 10(9), 797; https://doi.org/10.3390/cryst10090797 - 09 Sep 2020
Abstract
Biomineralization is a process in which specialized cells secrete and deliver inorganic ions into confined spaces limited by organic matrices or scaffolds. Chicken eggshell is the fastest biomineralization system on earth, and therefore, it is a good experimental model for the study of [...] Read more.
Biomineralization is a process in which specialized cells secrete and deliver inorganic ions into confined spaces limited by organic matrices or scaffolds. Chicken eggshell is the fastest biomineralization system on earth, and therefore, it is a good experimental model for the study of biomineralization. Eggshell mineralization starts on specialized dispersed sites of the soft fibrillar eggshell membranes referred to as negatively charged keratan sulfate mammillae. However, the rest of the fibrillar eggshell membranes never mineralizes, although 21% of their amino acids are acidic. We hypothesized that, relative to the mammillae, the negatively charged amino acids of the fibrillar eggshell membranes are not competitive enough to promote calcite nucleation and growth. To test this hypothesis, we experimentally increased the number of negatively charged carboxylate groups on the eggshell membrane fibers and compared it with in vitro calcite deposition of isolated intact eggshell membranes. We conclude that the addition of poly-carboxylated groups onto eggshell membranes increases the number of surface nucleation sites but not the crystal size. Full article
(This article belongs to the Special Issue Proteins and Biomineralisation)
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Review

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Open AccessReview
Glycosylation: A “Last Word” in the Protein-Mediated Biomineralization Process
Crystals 2020, 10(9), 818; https://doi.org/10.3390/cryst10090818 - 16 Sep 2020
Abstract
Post-translational modifications are one way that biomineral-associated cells control the function and fate of proteins. Of the ten different types of post-translational modifications, one of the most interesting and complex is glycosylation, or the covalent attachment of carbohydrates to amino acid sidechains Asn, [...] Read more.
Post-translational modifications are one way that biomineral-associated cells control the function and fate of proteins. Of the ten different types of post-translational modifications, one of the most interesting and complex is glycosylation, or the covalent attachment of carbohydrates to amino acid sidechains Asn, Ser, and Thr of proteins. In this review the author surveys some of the known biomineral-associated glycoproteins and summarizes recent in vitro recombinant protein experiments which test the impact of glycosylation on biomineralization protein functions, such as nucleation, crystal growth, and matrix assembly. These in vitro studies show that glycosylation does not alter the inherent function of the polypeptide chain; rather, it either accentuates or attenuates functionality. In essence, glycosylation gives the cell the “last word” as to what degree a biomineralization protein will participate in the biomineralization process. Full article
(This article belongs to the Special Issue Proteins and Biomineralisation)
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Open AccessReview
Structural Biology of Calcium Phosphate Nanoclusters Sequestered by Phosphoproteins
Crystals 2020, 10(9), 755; https://doi.org/10.3390/cryst10090755 - 27 Aug 2020
Abstract
Biofluids that contain stable calcium phosphate nanoclusters sequestered by phosphopeptides make it possible for soft and hard tissues to co-exist in the same organism with relative ease. The stability diagram of a solution of nanocluster complexes shows how the minimum concentration of phosphopeptide [...] Read more.
Biofluids that contain stable calcium phosphate nanoclusters sequestered by phosphopeptides make it possible for soft and hard tissues to co-exist in the same organism with relative ease. The stability diagram of a solution of nanocluster complexes shows how the minimum concentration of phosphopeptide needed for stability increases with pH. In the stable region, amorphous calcium phosphate cannot precipitate. Nevertheless, if the solution is brought into contact with hydroxyapatite, the crystalline phase will grow at the expense of the nanocluster complexes. The physico-chemical principles governing the formation, composition, size, structure, and stability of the complexes are described. Examples are given of complexes formed by casein, osteopontin, and recombinant phosphopeptides. Application of these principles and properties to blood serum, milk, urine, and resting saliva is described to show that under physiological conditions they are in the stable region of their stability diagram and so cannot cause soft tissue calcification. Stimulated saliva, however, is in the metastable region, consistent with its role in tooth remineralization. Destabilization of biofluids, with consequential ill-effects, can occur when there is a failure of homeostasis, such as an increase in pH without a balancing increase in the concentration of sequestering phosphopeptides. Full article
(This article belongs to the Special Issue Proteins and Biomineralisation)
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