Selected Papers From the 3rd International Electronic Conference on Biomolecules

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (31 January 2025) | Viewed by 2304

Special Issue Editors


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Department of Molecular Medicine and USF Health Byrd Alzheimer's Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA
Interests: protein physics; protein folding; protein misfolding; intrinsically disordered proteins; protein function; protein interactions
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CSIC Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Santander, Spain
Interests: Ras-ERK pathway spatial regulation; scaffold proteins; protein-protein interactions as therapeutic targets
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Special Issue Information

Dear Colleagues,

The 3rd International Electronic Conference on Biomolecules (IECBM 2024) (https://sciforum.net/event/IECBM2024) is organized by the MDPI open access journal Biomolecules (Impact Factor 4.8) and was held online from 23 to 25 Apr 2024. This conference aimed to provide leading scientists working in the field with an online platform on which to share their latest research and engage in exciting discussions. The main topics of the conference are as follows:

  1. Biomolecular Structures and Functions
  2. Molecular Mechanisms in Cellular Processes
  3. Biomolecular Interactions and Networks
  4. Biomaterials Design and Characterization
  5. Biocatalysis and Enzyme Engineering
  6. Bioinformatics and Computational Biology

Here are the key time points of the conference:

- Abstract Submission: 23rd January 2024
- Acceptance Notification: 23rd February 2024
- Early Bird Registration: 27th February 2024
- Registration Deadline: 17th April 2024
- Covering Author Registration: 23rd March 2024

This Special Issue is intended to collect the extended and expanded versions of the proceedings papers from the conference. All the conference participants will be granted a 20% discount on the Article Processing Charges (APC).

Prof. Dr. Vladimir N. Uversky
Prof. Dr. Piero Crespo
Guest Editors

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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.

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Published Papers (1 paper)

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Research

19 pages, 8357 KiB  
Article
Binding of Pro-Inflammatory Proteins S100A8 or S100A9 to Amyloid-β Peptide Suppresses Its Fibrillation
by Ekaterina A. Litus, Marina P. Shevelyova, Alisa A. Vologzhannikova, Evgenia I. Deryusheva, Andrey V. Machulin, Ekaterina L. Nemashkalova, Maria E. Permyakova, Andrey S. Sokolov, Valeria D. Alikova, Vladimir N. Uversky and Sergei E. Permyakov
Biomolecules 2025, 15(3), 431; https://doi.org/10.3390/biom15030431 - 17 Mar 2025
Viewed by 681
Abstract
Human serum albumin (HSA) is a natural depot of amyloid-β peptide (Aβ), a key player in Alzheimer’s disease (AD). HSA and pro-inflammatory Ca2+-binding proteins S100A8 and S100A9 are involved in Aβ metabolism and its deposition in the brain, serving as probable [...] Read more.
Human serum albumin (HSA) is a natural depot of amyloid-β peptide (Aβ), a key player in Alzheimer’s disease (AD). HSA and pro-inflammatory Ca2+-binding proteins S100A8 and S100A9 are involved in Aβ metabolism and its deposition in the brain, serving as probable triggers and therapeutic targets in AD, but their interplay with regard to Aβ binding/fibrillation is unclear. To this end, here we explore the in vitro binding of Ca2+-bound S100A8 or S100A9 to monomeric Aβ and the influence of the S100 proteins on Aβ fibrillation. The equilibrium dissociation constants of the complexes of dimeric S100A8/S100A9 with Aβ40/42 estimated by biolayer interferometry are 1–5 µM. S100A8 and S100A9 interfere with HSA binding to Aβ. Thioflavin T assay and electron microscopy data show that micromolar S100A8/S100A9 inhibit Aβ40 fibrillation, and the inhibitory effect of S100A8 exceeds that for HSA. The competition for Aβ between HSA and S100A8/S100A9 may contribute to the Aβ-HSA imbalance in the pro-inflammatory conditions in AD. Full article
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