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Biomolecules
Special Issues
CSF N- and O- Glycomics and Glycoproteomics
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CSF N- and O- Glycomics and Glycoproteomics

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 6870

Special Issue Editor

Dr. Domenico Garozzo

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Guest Editor
Institute for Polymers, Composites and Biomaterials (IPCB CNR) of Catania, Catania, Italy
Interests: glycomics; mass spectrometry; polysaccharides; lipopolysaccharides; structural elucidation; congenital glycosylation defects; neurodegenerative diseases

Special Issue Information

Dear Colleagues,

Cerebrospinal fluid (CSF) is an exceptionally fascinating matrix for the study of neurodegeneration, since it has direct contact with the brain and the spinal cord and biochemical changes occurring during disease progression can be disclosed in the cerebrospinal fluid. Therefore, CSF glycomics and glycoproteomics together represent a reliable and feasible approach for the characterization of the brain glycoproteome, enabling the identification of possible alterations on different pathological processes affecting the central nervous system.

Glycosylation changes in Alzheimer’s disease, leukodystrophies, GM2 gangliosidosis, schizophrenia, and other diseases have been recently reported. This Special Issue aims to obtain a global view on the state of N- and O-glycosylation for the discovery of neurodegeneration biomarkers and/or potential pharmaceutical targets.

Dr. Domenico Garozzo
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. Biomolecules 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 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

  • cerebrospinal fluid (CSF)
  • glycomics
  • glycoproteomics
  • neurodegeneration

Published Papers (2 papers)

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Research

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14 pages, 2309 KiB  
Article
Trehalose Restrains the Fibril Load towards α-Lactalbumin Aggregation and Halts Fibrillation in a Concentration-Dependent Manner
by Sania Bashir, Ishfaq Ahmad Ahanger, Anas Shamsi, Mohamed F. Alajmi, Afzal Hussain, Hani Choudhry, Faizan Ahmad, Md. Imtaiyaz Hassan and Asimul Islam
Biomolecules 2021, 11(3), 414; https://doi.org/10.3390/biom11030414 - 11 Mar 2021
Cited by 12 | Viewed by 2902
Abstract
Protein aggregation and misfolding are some of the most challenging obstacles, customarily studied for their association with amyloid pathologies. The mechanism of amyloid fibrillation development is a dynamic phenomenon involving various factors such as the intrinsic properties of protein and the physical and [...] Read more.
Protein aggregation and misfolding are some of the most challenging obstacles, customarily studied for their association with amyloid pathologies. The mechanism of amyloid fibrillation development is a dynamic phenomenon involving various factors such as the intrinsic properties of protein and the physical and chemical environmental conditions. The purpose of this study was to see the thermal aggregation profile of alpha-lactalbumin (α-LA) and to delineate the effect of trehalose on its aggregation profile. α-LA was subjected to thermal aggregation at high concentrations. UV-Vis spectroscopy, a turbidity assay, intrinsic fluorescence, Rayleigh scattering and a thioflavin T (ThT) assay explained the steady outcomes that 1 M trehalose repressed α-LA aggregation in the most effective way followed by 0.75 M and 0.5 M and to a significantly lesser degree by 0.25 M. Multi spectroscopic obser Sania Bashir ations were further entrenched by microscopy. Transmission electron microscopy confirmed that in the presence of its higher concentration, trehalose hinders fibril development in α-LA. In vitro studies were further validated by in silico studies. Molecular docking analysis indicated that trehalose occupied the binding pocket cavity of α-LA and offered several significant interactions, including H-bonds with important residues. This study provides a platform for trehalose in the therapeutic management of protein aggregation-related diseases. Full article
(This article belongs to the Special Issue CSF N- and O- Glycomics and Glycoproteomics)
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Review

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21 pages, 10577 KiB  
Review
What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
by Stefan Gaunitz, Lars O. Tjernberg and Sophia Schedin-Weiss
Biomolecules 2021, 11(6), 858; https://doi.org/10.3390/biom11060858 - 9 Jun 2021
Cited by 10 | Viewed by 3292
Abstract
Proteomics—large-scale studies of proteins—has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease. To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the “omics”. To this [...] Read more.
Proteomics—large-scale studies of proteins—has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease. To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the “omics”. To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest. The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered. Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies. Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls. In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid. Full article
(This article belongs to the Special Issue CSF N- and O- Glycomics and Glycoproteomics)
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