Proteins and Peptides (Closed)

A topical collection in Polymers (ISSN 2073-4360). This collection belongs to the section "Biomacromolecules, Biobased and Biodegradable Polymers".

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Editors


E-Mail Website1 Website2
Collection Editor
Advanced Polymer Materials Group, Department of Bioresources and Polymer Science, Politehnica University of Bucharest, 011061 Bucharest, Romania
Interests: protein structure; protein function; protein folding; protein-synthetic polymers interaction; protein-based complexes for tissue engineering; protein-based biomaterials
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grade E-Mail Website
Collection Editor
Department of Molecular Medicine, University of South Florida, Tampa, FL, USA
Interests: protein folding; protein misfolding; intrinsically disordered proteins
Special Issues, Collections and Topics in MDPI journals

Topical Collection Information

Dear Colleagues,

The protein/peptide structure–function relationship represents a key problem at the cross-section between modern biochemistry, biophysics, molecular biology, and medicine. The importance of protein and peptides cannot be overestimated, as they are the major functional and structural components of the living cell that play a number of crucial roles in the maintenance of life. Proteins may serve as simple structural blocks, supporting cellular shape, or may be involved in catalysis of various biological reactions, or energy interconversion, or, together with peptides, they can be involved in signal transduction and transmission of information. Peptides are commonly involved in the regulation of various biological processes. Proteins and peptides might act alone or in complexes with various partners. Dysfunctions of many proteins and peptides are associated with the pathogenesis of various diseases. The main goal of this Topic Collection is to provide a platform for reporting studies in the field of protein/peptide structure and function as well as research concerning proteins engineering domain with multiple focus on advanced biomedical applications.  

Prof. Dr. Horia Iovu
Dr. Vladimir N. Uversky
Collection Editors

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Keywords

  • protein structure
  • protein function
  • protein folding
  • protein misfolding
  • intrinsically disordered proteins
  • proteins engineering

Published Papers (1 paper)

2022

23 pages, 2464 KiB  
Review
Graphene Oxide–Protein-Based Scaffolds for Tissue Engineering: Recent Advances and Applications
by Elena Iuliana Biru, Madalina Ioana Necolau, Adriana Zainea and Horia Iovu
Polymers 2022, 14(5), 1032; https://doi.org/10.3390/polym14051032 - 4 Mar 2022
Cited by 32 | Viewed by 4592
Abstract
The field of tissue engineering is constantly evolving as it aims to develop bioengineered and functional tissues and organs for repair or replacement. Due to their large surface area and ability to interact with proteins and peptides, graphene oxides offer valuable physiochemical and [...] Read more.
The field of tissue engineering is constantly evolving as it aims to develop bioengineered and functional tissues and organs for repair or replacement. Due to their large surface area and ability to interact with proteins and peptides, graphene oxides offer valuable physiochemical and biological features for biomedical applications and have been successfully employed for optimizing scaffold architectures for a wide range of organs, from the skin to cardiac tissue. This review critically focuses on opportunities to employ protein–graphene oxide structures either as nanocomposites or as biocomplexes and highlights the effects of carbonaceous nanostructures on protein conformation and structural stability for applications in tissue engineering and regenerative medicine. Herein, recent applications and the biological activity of nanocomposite bioconjugates are analyzed with respect to cell viability and proliferation, along with the ability of these constructs to sustain the formation of new and functional tissue. Novel strategies and approaches based on stem cell therapy, as well as the involvement of the extracellular matrix in the design of smart nanoplatforms, are discussed. Full article
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