Special Issue "Noncovalent Interactions in Biomolecules"

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

Deadline for manuscript submissions: 20 March 2022.

Special Issue Editor

Dr. Antonio Bauzá
E-Mail Website
Guest Editor
Departament de Química, Universitat de les Illes Balears, Palma de Mallorca, 07122 Baleares, Spain
Interests: noncovalent interactions; supramolecular chemistry; Lewis acid–Lewis base interactions; crystal engineering; theoretical chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Noncovalent interactions (NCIs) are very important in many different fields of modern chemistry (e.g., supramolecular chemistry, crystal engineering or molecular sensing). Apart from classical noncovalent forces (hydrogen bond, p-p stacking, and cation/anion–p interactions), a novel class of noncovalent bonds has been described and characterized (mostly from theoreticians) during the past decade. It refers to the formation of σ- or π-holes in atoms belonging to the p-block of elements, which can undergo attractive interactions with any electron-rich site.

In a biological context, it is of crucial importance to advance the knowledge regarding the interplay between these tight binding forces, since it is the main driving force of complex biological phenomena, such as protein folding or protein–protein recognition mechanisms. In order to move forward in this direction, a more focused approach is needed regarding the analysis of NCIs in biological systems. Many biological studies (mostly related to protein–ligand interactions) have highlighted the role of both classical and novel NCIs in the formation and stability of biological complexes. However, more information and examples are needed regarding protein–protein or transmembrane protein complexes among other biological assemblies.

We invite researchers to contribute to the Special Issue on NCIs in biomolecules, which is intended to serve as a unique multidisciplinary forum covering all aspects of noncovalent interactions involving both classical and novel noncovalent bonds in a biological context.

The potential topics include but are not limited to the following:

Description, analysis, and theoretical studies of biologically relevant assemblies

Structure and properties of new biological complexes where NCIs play a key role

Enzyme chemistry based on noncovalent bonding

Dr. Antonio Bauzá
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 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 2000 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

  • Protein complexes
  • Noncovalent interactions
  • Supramolecular assemblies
  • Hydrogen bonding
  • Enzyme chemistry
  • Anion-π

Published Papers (3 papers)

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Research

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Article
The Crystal Structure Elucidation of a Tetrapeptide Analog of Somatostatin DOTA-Phe-D-Trp-Lys-Thr-OMe
Crystals 2022, 12(1), 12; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst12010012 - 22 Dec 2021
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Abstract
Herewith, we report for the first time the crystal structure of tetrapeptide FwKT (Phe-D-Trp-Lys-Thr), which is considered to represent an epitope for biomedically relevant hormone somatostatin. The target molecule was successfully crystalized, solved and refined as a conjugate of the tetrapeptide moiety bearing [...] Read more.
Herewith, we report for the first time the crystal structure of tetrapeptide FwKT (Phe-D-Trp-Lys-Thr), which is considered to represent an epitope for biomedically relevant hormone somatostatin. The target molecule was successfully crystalized, solved and refined as a conjugate of the tetrapeptide moiety bearing a protective group DOTA at the N-terminus and methylated at the O-terminus. The combination of a hormone active site and a powerful chelator make the substance a highly prospective targeted drug delivery system, especially for peptide receptor radionuclide therapy (PRRT) applications. Full article
(This article belongs to the Special Issue Noncovalent Interactions in Biomolecules)
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Article
Synthesis, Structure and Evaluation of the N-(2-Acetyl-4-(styryl)phenyl)-4-benzenesulfonamide Derivatives for Anticholinesterase and Antioxidant Activities
Crystals 2021, 11(4), 341; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst11040341 - 28 Mar 2021
Cited by 3 | Viewed by 603
Abstract
N-(2-Acetyl-4-bromophenyl)-4-methylbenzenesulfonamide (2) was transformed into 5-(4-methoxymethylstyryl)-2-(p-tolylsulfonamido)acetophenone (3a) and 5-(4- trifluoromethylstyryl)-2-(p-tolylsulfonamido)acetophenone (3b). Their structures were determined using a combination of NMR (1H & 13C) and mass spectroscopic as well as [...] Read more.
N-(2-Acetyl-4-bromophenyl)-4-methylbenzenesulfonamide (2) was transformed into 5-(4-methoxymethylstyryl)-2-(p-tolylsulfonamido)acetophenone (3a) and 5-(4- trifluoromethylstyryl)-2-(p-tolylsulfonamido)acetophenone (3b). Their structures were determined using a combination of NMR (1H & 13C) and mass spectroscopic as well as single crystal X-ray diffraction techniques. These compounds and the corresponding precursor, 2-amino-5-bromoacetophenone (1), were evaluated through enzymatic assays in vitro for inhibitory effect against acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) activities as well as antioxidant effect through the 2,2-diphenyl-1-picrylhydrazyl (DPPH) and nitric oxide (NO) free radical scavenging assays. Molecular docking was performed on 3a to determine plausible protein–ligand interactions on a molecular level. Their drug likeness properties (absorption, distribution, metabolism, and excretion) and ability to cross the blood–brain barrier (BBB) have also been predicted at theoretical level. Full article
(This article belongs to the Special Issue Noncovalent Interactions in Biomolecules)
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Review

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Review
Tryptophan, an Amino-Acid Endowed with Unique Properties and Its Many Roles in Membrane Proteins
Crystals 2021, 11(9), 1032; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst11091032 - 27 Aug 2021
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Abstract
Tryptophan is an aromatic amino acid with unique physico-chemical properties. It is often encountered in membrane proteins, especially at the level of the water/bilayer interface. It plays a role in membrane protein stabilization, anchoring and orientation in lipid bilayers. It has a hydrophobic [...] Read more.
Tryptophan is an aromatic amino acid with unique physico-chemical properties. It is often encountered in membrane proteins, especially at the level of the water/bilayer interface. It plays a role in membrane protein stabilization, anchoring and orientation in lipid bilayers. It has a hydrophobic character but can also engage in many types of interactions, such as π–cation or hydrogen bonds. In this review, we give an overview of the role of tryptophan in membrane proteins and a more detailed description of the underlying noncovalent interactions it can engage in with membrane partners. Full article
(This article belongs to the Special Issue Noncovalent Interactions in Biomolecules)
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