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Magnetochemistry
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Nuclear Magnetic Resonance Spectroscopy in Biomedical Application
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Nuclear Magnetic Resonance Spectroscopy in Biomedical Application

A special issue of Magnetochemistry (ISSN 2312-7481). This special issue belongs to the section "Magnetic Resonances".

Deadline for manuscript submissions: closed (15 September 2020) | Viewed by 20256

Special Issue Editor

Dr. Teresa Lehmann

E-Mail Website
Guest Editor
Department of Chemistry, University of Wyoming, Laramie, WY 82071, USA
Interests: NMR; cancer drugs; malaria; solution structure determination; interfacial phenomena; colloidal dispersion gels
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique that can be used to investigate the structure, dynamics, and chemical kinetics of a wide range of biomolecular systems. The development of cutting edge NMR methods in the last 30 years has revolutionized our ability to characterize biological macromolecules. The accelerated progress of NMR applied to biomolecules has lifted some previous limitations regarding molecular size, solubility and abundance, which used to hinder biopolymer-structure determination. NMR has emerged from being a measuring tool used only in chemistry and physics to become a widely used techniques in all areas of biological science, medical diagnosis, and clinical investigation. This Special Issue of the open access journal, Magnetochemistry, devoted to “Nuclear Magnetic Resonance Spectroscopy in Biomedical Applications”, will provide researches in the field with the opportunity to publish their most recent discoveries using this exciting technique.

Dr. Teresa Lehmann
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.

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Published Papers (5 papers)

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Research

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13 pages, 3116 KiB  
Article
Structural Characterization of the S-glycosylated Bacteriocin ASM1 from Lactobacillus plantarum
by Alexander K. Goroncy, Trevor S. Loo, Adrian M. Koolaard, Mark L. Patchett and Gillian E. Norris
Magnetochemistry 2020, 6(1), 16; https://doi.org/10.3390/magnetochemistry6010016 - 22 Mar 2020
Cited by 4 | Viewed by 4523
Abstract
In order to protect their environmental niche, most bacteria secret antimicrobial substances designed to target specific bacterial strains that are often closely related to the producer strain. Bacteriocins, small, ribosomally synthesised antimicrobial peptides, comprise a class of such substances and can either inhibit [...] Read more.
In order to protect their environmental niche, most bacteria secret antimicrobial substances designed to target specific bacterial strains that are often closely related to the producer strain. Bacteriocins, small, ribosomally synthesised antimicrobial peptides, comprise a class of such substances and can either inhibit (bacteriostatic) or kill (bactericidal) target cells. Glycocins are a class of bacteriocin that are post-translationally modified by one or more carbohydrate moieties that are either β-O-linked to either a serine or threonine and/or β-S-linked to a cysteine. The solution nuclear magnetic resonance structure (NMR) of the glycocin ASM1 (produced by Lactobacillus plantarum A-1), an orthologue of GccF, has been determined. In both structures, the disulfide bonds are essential for activity and restrict the mobility of the N-acetyl-glucosamine (GlcNAc) attached to Ser-18 (O-linked), compared to the much more flexible GlcNAc moiety on Cys-43 (S-linked). Interestingly, despite 88% sequence identity, the helical structure of ASM1 is less pronounced which appears to be consistent with the far ultra-violet circular dichroism (UV CD) spectra. Full article
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy in Biomedical Application)
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15 pages, 4549 KiB  
Article
Disturbance of the Conformation of DNA Hairpin Containing the 5′-GT-3′ Binding Site Caused by Zn(II)bleomycin-A5 Studied through NMR Spectroscopy
by Kyle L. Covington and Teresa Lehmann
Magnetochemistry 2019, 5(3), 52; https://doi.org/10.3390/magnetochemistry5030052 - 8 Sep 2019
Viewed by 3126
Abstract
The antibiotics known as bleomycins constitute a family of natural products clinically employed for the treatment of a wide spectrum of cancers. These antibiotics have the ability to chelate a metal center, most commonly Fe(II), and cause site-specific DNA cleavage upon oxidation. Bleomycin [...] Read more.
The antibiotics known as bleomycins constitute a family of natural products clinically employed for the treatment of a wide spectrum of cancers. These antibiotics have the ability to chelate a metal center, most commonly Fe(II), and cause site-specific DNA cleavage upon oxidation. Bleomycin therapy is a successful course of treatment for some types of cancers. However, the risk of pulmonary fibrosis as an undesirable side effect, limits the use of the antibiotics in cancer chemotherapy. Bleomycins are differentiated by their C-terminal, or tail, regions, which have been shown to closely interact with DNA. Pulmonary toxicity has been correlated to the chemical structure of the bleomycin C-termini through biochemical studies performed in mice. In the present study, we examined the binding of Zn(II)Bleomycin-A5 to a DNA hairpin of sequence 5′-CCAGTATTTTTACTGG-3′, containing the 5′-GT-3′ binding site. The results were compared to those from a previous study that examined the binding of Zn(II)Bleomycin-A2 and Zn(II)Peplomycin to the same DNA hairpin. We provide evidence that, as shown for DNA hairpins containing the 5′-GC-3′ binding site, Zn(II)BLM-A5 causes the most significant structural changes to the oligonucleotide. Full article
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy in Biomedical Application)
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6 pages, 1291 KiB  
Communication
Sensitive Water Ligand Observed via Gradient Spectroscopy with 19F Detection for Analysis of Fluorinated Compounds Bound to Proteins
by Kazuo Furihata and Mitsuru Tashiro
Magnetochemistry 2019, 5(2), 29; https://doi.org/10.3390/magnetochemistry5020029 - 1 May 2019
Cited by 6 | Viewed by 2733
Abstract
The water ligand observed via a gradient spectroscopy type experiment with 19F detection was applied to selectively detect fluorinated compounds with affinity to the target proteins. The 19F signals of bound and unbound compounds were observed as opposite phases, which was [...] Read more.
The water ligand observed via a gradient spectroscopy type experiment with 19F detection was applied to selectively detect fluorinated compounds with affinity to the target proteins. The 19F signals of bound and unbound compounds were observed as opposite phases, which was advantageous to distinguish the binding state. The proposed NMR method was optimized based on the 19F{1H} saturation transfer difference pulse sequence, and various inversion pulses for the water resonance were evaluated with the aim of high sensitivity. Full article
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy in Biomedical Application)
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Review

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21 pages, 1834 KiB  
Review
Paramagnetic NMR Spectroscopy Is a Tool to Address Reactivity, Structure, and Protein–Protein Interactions of Metalloproteins: The Case of Iron–Sulfur Proteins
by Mario Piccioli
Magnetochemistry 2020, 6(4), 46; https://doi.org/10.3390/magnetochemistry6040046 - 26 Sep 2020
Cited by 12 | Viewed by 4539
Abstract
The study of cellular machineries responsible for the iron–sulfur (Fe–S) cluster biogenesis has led to the identification of a large number of proteins, whose importance for life is documented by an increasing number of diseases linked to them. The labile nature of Fe–S [...] Read more.
The study of cellular machineries responsible for the iron–sulfur (Fe–S) cluster biogenesis has led to the identification of a large number of proteins, whose importance for life is documented by an increasing number of diseases linked to them. The labile nature of Fe–S clusters and the transient protein–protein interactions, occurring during the various steps of the maturation process, make their structural characterization in solution particularly difficult. Paramagnetic nuclear magnetic resonance (NMR) has been used for decades to characterize chemical composition, magnetic coupling, and the electronic structure of Fe–S clusters in proteins; it represents, therefore, a powerful tool to study the protein–protein interaction networks of proteins involving into iron–sulfur cluster biogenesis. The optimization of the various NMR experiments with respect to the hyperfine interaction will be summarized here in the form of a protocol; recently developed experiments for measuring longitudinal and transverse nuclear relaxation rates in highly paramagnetic systems will be also reviewed. Finally, we will address the use of extrinsic paramagnetic centers covalently bound to diamagnetic proteins, which contributed over the last twenty years to promote the applications of paramagnetic NMR well beyond the structural biology of metalloproteins. Full article
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy in Biomedical Application)
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10 pages, 1381 KiB  
Review
Magnetic Nanoparticles as In Vivo Tracers for Alzheimer’s Disease
by Bhargy Sharma and Konstantin Pervushin
Magnetochemistry 2020, 6(1), 13; https://doi.org/10.3390/magnetochemistry6010013 - 4 Mar 2020
Cited by 11 | Viewed by 4364
Abstract
Drug formulations and suitable methods for their detection play a very crucial role in the development of therapeutics towards degenerative neurological diseases. For diseases such as Alzheimer’s disease, magnetic resonance imaging (MRI) is a non-invasive clinical technique suitable for early diagnosis. In this [...] Read more.
Drug formulations and suitable methods for their detection play a very crucial role in the development of therapeutics towards degenerative neurological diseases. For diseases such as Alzheimer’s disease, magnetic resonance imaging (MRI) is a non-invasive clinical technique suitable for early diagnosis. In this review, we will discuss the different experimental conditions which can push MRI as the technique of choice and the gold standard for early diagnosis of Alzheimer’s disease. Here, we describe and compare various techniques for administration of nanoparticles targeted to the brain and suitable formulations of nanoparticles for use as magnetically active therapeutic probes in drug delivery targeting the brain. We explore different physiological pathways involved in the transport of such nanoparticles for successful entry in the brain. In our lab, we have used different formulations of iron oxide nanoparticles (IONPs) and protein nanocages as contrast agents in anatomical MRI of an Alzheimer’s disease (AD) brain. We compare these coatings and their benefits to provide the best contrast in addition to biocompatibility properties to be used as sustainable drug-release systems. In the later sections, the contrast enhancement techniques in MRI studies are discussed. Examples of contrast-enhanced imaging using advanced pulse sequences are discussed with the main focus on important studies in the field of neurological diseases. In addition, T1 contrast agents such as gadolinium chelates are compared with the T2 contrast agents mainly made of superparamagnetic inorganic metal nanoparticles. Full article
(This article belongs to the Special Issue Nuclear Magnetic Resonance Spectroscopy in Biomedical Application)
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