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Special Issue "Advanced Research of Amyloids"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 1 January 2022.

Special Issue Editor

Prof. Dr. Yifat Miller
E-Mail Website
Guest Editor
Department of Chemistry and the Ilse Katz Institute for Nanoscale Science & Technology, Ben-Gurion University of the Negev, Beer Sheva, Israel
Interests: molecular dynamics simulations; amyloid aggregation; amyloid–metal interactions; peptides and metal–peptide interactions; self-assembly; Alzheimer's; Parkinson's; type 2 diabetes

Special Issue Information

Dear Colleagues,

The field of research of amyloid diseases is rapidly expanding and is conducted in many different disciplines. This Special Issue will promote interdisciplinary research activity in this important field. The amyloid diseases have become the heaviest load on the economy of the medical services in the developed world, rendering major social and economic importance to any progress in understanding the molecular, cellular, and organismic factors involved in the onset and treatment of these diseases.

It is my pleasure to invite you to submit a research article, short communication, or review article to this Special Issue. This Special Issue will focus on recent advances in research on amyloid proteins, including microbial amyloids, using a variety of studies: in vivo, in vitro, molecular biology, and in silico. This Issue will cover a wide spectrum of topics related to advanced methods for the structural biology of amyloids, the molecular mechanisms and kinetics of amyloid aggregation, the role of metals in amyloid aggregation, the molecular affinity of amyloids with lipid membranes, and novel therapeutic strategies in amyloid diseases.

I look forward to receiving your contributions to this exciting Special Issue.

Prof. Dr. Yifat Miller
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • neurodegeneration
  • amyloids oligomers
  • amyloid fibrils
  • NMR
  • crystal structure
  • molecular mechanisms
  • amyloid–membrane interactions
  • drug design
  • inhibitors

Published Papers (1 paper)

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Research

Article
Multiscale Modeling of Amyloid Fibrils Formed by Aggregating Peptides Derived from the Amyloidogenic Fragment of the A-Chain of Insulin
Int. J. Mol. Sci. 2021, 22(22), 12325; https://doi.org/10.3390/ijms222212325 - 15 Nov 2021
Viewed by 339
Abstract
Computational prediction of molecular structures of amyloid fibrils remains an exceedingly challenging task. In this work, we propose a multi-scale modeling procedure for the structure prediction of amyloid fibrils formed by the association of ACC1-13 aggregation-prone peptides derived from the N-terminal region [...] Read more.
Computational prediction of molecular structures of amyloid fibrils remains an exceedingly challenging task. In this work, we propose a multi-scale modeling procedure for the structure prediction of amyloid fibrils formed by the association of ACC1-13 aggregation-prone peptides derived from the N-terminal region of insulin’s A-chain. First, a large number of protofilament models composed of five copies of interacting ACC1-13 peptides were predicted by application of CABS-dock coarse-grained (CG) docking simulations. Next, the models were reconstructed to all-atom (AA) representations and refined during molecular dynamics (MD) simulations in explicit solvent. The top-scored protofilament models, selected using symmetry criteria, were used for the assembly of long fibril structures. Finally, the amyloid fibril models resulting from the AA MD simulations were compared with atomic force microscopy (AFM) imaging experimental data. The obtained results indicate that the proposed multi-scale modeling procedure is capable of predicting protofilaments with high accuracy and may be applied for structure prediction and analysis of other amyloid fibrils. Full article
(This article belongs to the Special Issue Advanced Research of Amyloids)
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