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Symmetry
Special Issues
Functional Materials Engineering and Biomolecular Structure
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Functional Materials Engineering and Biomolecular Structure

A special issue of Symmetry (ISSN 2073-8994). This special issue belongs to the section "Chemistry: Symmetry/Asymmetry".

Deadline for manuscript submissions: closed (30 June 2021) | Viewed by 4493

Special Issue Editor

Prof. Dr. Robert Wieczorek

E-Mail Website
Guest Editor
Dipartimento di Chimica e Tecnologie Chimiche, Università della Calabria, 87030 Arcavacata di Rende (CS), Italy
Interests: functional materials engineering; biomolecular structure; structure - properties relationship

Special Issue Information

Dear Colleagues,

In recent years, we have observed an extremely dynamic increase in interest in interdisciplinary research, in which chemistry is an integral and often leading part of research. The results of interdisciplinary research in the field of new materials engineering and predicting the properties of biochemical systems are not only cognitively fascinating but also promising in the context of potential applications. In particular, a design of new materials that can serve as energy storage media or light sources is in the area of interest of the largest scientific agencies, reflecting the needs of modern society. On the other hand, the biol–chem–med three-way marriage requires studying and effectively predicting the biomolecular structure as a useful source of information about molecules and their roles in living organisms. It is an important step on the ladder that we climb together to answer important questions, in particular about diseases that we would like to prevent and treat.

In this Special Issue, we will focus on presenting current research trends and reviewing the possibilities of modern science in the area of “Functional Materials Engineering and Biomolecular Structure”.

Please note that all of the submitted papers must be within the general scope of the Symmetry journal.

Prof. Robert Wieczorek
Guest Editor

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 submissions that pass pre-check are 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. Symmetry 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 2400 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

  • functional materials engineering
  • biomolecular structure
  • structure–properties relationship

Published Papers (2 papers)

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Research

12 pages, 4341 KiB  
Article
Interactions of Aβ1-42 Peptide and Its Three Fragments (Aβ8-12, Aβ8-13, and Aβ5-16) with Selected Nonsteroidal Drugs and Compounds of Natural Origin
by Krzysztof Żamojć, Karolina Streńska, Dariusz Wyrzykowski, Lech Chmurzyński and Joanna Makowska
Symmetry 2020, 12(10), 1579; https://doi.org/10.3390/sym12101579 - 23 Sep 2020
Viewed by 1720
Abstract
In the following paper, we present the results of our studies on the interactions of the Aβ1-42 peptide and its three short fragments, namely Aβ5-16 (RHDSGYEVHHQK; HZ1), Aβ8-13 (SGYEVH; HZ2), and Aβ8-12 (SGYEV; HZ3) with selected painkillers (ibuprofen and [...] Read more.
In the following paper, we present the results of our studies on the interactions of the Aβ1-42 peptide and its three short fragments, namely Aβ5-16 (RHDSGYEVHHQK; HZ1), Aβ8-13 (SGYEVH; HZ2), and Aβ8-12 (SGYEV; HZ3) with selected painkillers (ibuprofen and aspirin) and compounds of natural origin (anabasine and epinephrine). Steady-state fluorescence spectroscopy was used to study the binding properties of the selected systems. Additionally, based on molecular dynamics (MD) calculations supported by NMR-derived restrains, we have proposed the most likely area of the interactions of Aβ1-42 and Aβ5-16 peptides with the investigated compounds. The influence of symmetrically oriented side chains of amino acid residues present in the first part of the Aβ1-42 sequence on the stability of the resulting complexes has been discussed. Finally, the changes in the peptide structures on account of complex formation were analyzed. Full article
(This article belongs to the Special Issue Functional Materials Engineering and Biomolecular Structure)
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11 pages, 1395 KiB  
Article
Tripodal Podand Ligand with a Superhalogen Nature as an Effective Molecular Trap
by Adrianna Cyraniak and Marcin Czapla
Symmetry 2020, 12(9), 1441; https://doi.org/10.3390/sym12091441 - 1 Sep 2020
Cited by 3 | Viewed by 2422
Abstract
Tris(2-methoxyethyl) fluoroborate anion (TMEFA), anovel tripodal ligand based on the BF4− superhalogen anion, is proposed and was investigated theoretically using ab initio MP2 (second-order Møller-Plesset perturbational method) and OVGF (outer valence Green function) methods. The studied molecule comprises three 2-methoxyethoxy groups [...] Read more.
Tris(2-methoxyethyl) fluoroborate anion (TMEFA), anovel tripodal ligand based on the BF4− superhalogen anion, is proposed and was investigated theoretically using ab initio MP2 (second-order Møller-Plesset perturbational method) and OVGF (outer valence Green function) methods. The studied molecule comprises three 2-methoxyethoxy groups (-O-CH2-CH2-O-CH3) connected to a central boron atom, which results in the C3-symmetry of the compound. The resulting anion was stable against fragmentation processes and its vertical electron detachment energy was found to be 5.72 eV. Due to its equilibrium structure resembling that of classical tripodal podands, the [F-B(O-CH2-CH2-O-CH3)3]− anion is capable of binding metal cations using its three arms, and thus may form strongly bound ionic complexes such as [F-B(O-CH2-CH2-O-CH3)3]−/Li+ and [F-B(O-CH2-CH2-O-CH3)3]−/Mg2+. The binding energies predicted for such compounds far exceed those of the similar neutral classical podand ligands, which likely makes the [F-B(O-CH2-CH2-O-CH3)3]− system a more effective molecular trap or steric shielding agent with respect to selected metal cations. Full article
(This article belongs to the Special Issue Functional Materials Engineering and Biomolecular Structure)
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