Mechanisms of Formation of Biomolecule Complexes: Theory, Experiment, Applications

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Structure and Dynamics".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 2168

Special Issue Editors


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Guest Editor
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Krakow, Poland
Interests: adsorption kinetics via quartz crystal microbalance; biofunctionalisation; interfacial phenomena (self- assembly etc.); ZnO nanocrystalline film synthesis and functionalisation; FT-IRRAS

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Guest Editor
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, PL-30239 Krakow, Poland
Interests: biocompatible polyelectrolyte films; polysaccharides; biomaterials; application of electrokinetic techniques for determination of the properties of nanocomposites; binding proteins to polyelectrolyte multilayers; determination of the stability of polyelectrolyte mono- and multilayers; determination of the physicochemical properties of polyelectrolytes in bulk
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, PL-30239 Krakow, Poland
Interests: preparation and characterization of mono-, bi-, and multilayers of macroions and nanoparticles; mechanisms of macroion and nanoparticle adsorption; kinetics adsorption and desorption of macromolecules and nanoparticles; macroion adsorption at homogeneous and heterogeneous surfaces; stability of monolayers and bilayers composed of macromolecules and nanoparticles; biocompatibility of composed layered materials; electrokinetic potential at solid/liquid interfaces; streaming potential at solid/liquid interfaces; layer by layer deposition of colloidal particles; polypeptides and their monolayers; nanoparticles/macroions composite material; biological applications of macromolecules and nanoparticles
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Complexes are crucial in industrial applications because they can be employed in dialysis, ultrafiltration or seawater desalination, protein purification, growth factor delivery and encapsulating drugs. Control of the complex stability, and determination of their physicochemical properties and biological activity are especially important.

The Special Issue is devoted to the most recent research on the determination of formation mechanisms underlying biomolecule complexes. The process of combining proteins, polypeptides or biocompatible polyelectrolytes  into defined aggregates/ coacervates will be broadly discussed.

Despite the vital importance of biomolecule complexes in these fields, the mechanisms of formation of biomolecule complexes and kinetics of the immobilization processes of bioactive agents are not sufficiently understood nor described theoretically or experimentally in the literature.

To fill this gap, this Special Issue will cover the most recent research focused on these phenomena. Original articles, brief communications and review articles are invited.

Dr. Agata Pomorska
Dr. Aneta Michna
Dr. Maria Morga
Guest Editors

Manuscript Submission Information

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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.

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Keywords

  • biomolecule complexes
  • biomolecule coacervates
  • complex stability
  • mechanisms of formation of biomolecule complexes
  • phase separation
  • application of biomolecule complexes in biomedical industry

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Published Papers (2 papers)

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Research

13 pages, 2866 KiB  
Article
Complexes of HMO1 with DNA: Structure and Affinity
by Daria K. Malinina, Grigoriy A. Armeev, Olga V. Geraskina, Anna N. Korovina, Vasily M. Studitsky and Alexey V. Feofanov
Biomolecules 2024, 14(9), 1184; https://doi.org/10.3390/biom14091184 - 20 Sep 2024
Viewed by 763
Abstract
Saccharomyces cerevisiae HMO1 is an architectural nuclear DNA-binding protein that stimulates the activity of some remodelers and regulates the transcription of ribosomal protein genes, often binding to a DNA motif called IFHL. However, the molecular mechanism dictating this sequence specificity is unclear. Our [...] Read more.
Saccharomyces cerevisiae HMO1 is an architectural nuclear DNA-binding protein that stimulates the activity of some remodelers and regulates the transcription of ribosomal protein genes, often binding to a DNA motif called IFHL. However, the molecular mechanism dictating this sequence specificity is unclear. Our circular dichroism spectroscopy studies show that the HMO1:DNA complex forms without noticeable changes in the structure of DNA and HMO1. Molecular modeling/molecular dynamics studies of the DNA complex with HMO1 Box B reveal two extended sites at the N-termini of helices I and II of Box B that are involved in the formation of the complex and stabilize the DNA bend induced by intercalation of the F114 side chain between base pairs. A comparison of the affinities of HMO1 for 24 bp DNA fragments containing either randomized or IFHL sequences reveals a twofold increase in the stability of the complex in the latter case, which may explain the selectivity in the recognition of the IFHL-containing promoter regions. Full article
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16 pages, 6323 KiB  
Article
Kinetics of Human Serum Albumin Adsorption on Polycation Functionalized Silica
by Małgorzata Nattich-Rak, Dominik Kosior, Maria Morga and Zbigniew Adamczyk
Biomolecules 2024, 14(5), 531; https://doi.org/10.3390/biom14050531 - 29 Apr 2024
Cited by 1 | Viewed by 1045
Abstract
The adsorption kinetics of human serum albumin (HSA) on bare and poly-L-arginine (PARG)-modified silica substrates were investigated using reflectometry and atomic force microscopy (AFM). Measurements were carried out at various pHs, flow rates and albumin concentrations in the 10 and 150 mM NaCl [...] Read more.
The adsorption kinetics of human serum albumin (HSA) on bare and poly-L-arginine (PARG)-modified silica substrates were investigated using reflectometry and atomic force microscopy (AFM). Measurements were carried out at various pHs, flow rates and albumin concentrations in the 10 and 150 mM NaCl solutions. The mass transfer rate constants and the maximum protein coverages were determined for the bare silica at pH 4.0 and theoretically interpreted in terms of the hybrid random sequential adsorption model. These results were used as reference data for the analysis of adsorption kinetics at larger pHs. It was shown that the adsorption on bare silica rapidly decreased with pH and became negligible at pH 7.4. The albumin adsorption on PARG-functionalized silica showed an opposite trend, i.e., it was negligible at pH 4 and attained maximum values at pH 7.4 and 150 mM NaCl, the conditions corresponding to the blood serum environment. These results were interpreted as the evidence of a significant role of electrostatic interactions in the albumin adsorption on the bare and PARG-modified silica. It was also argued that our results can serve as useful reference data enabling a proper interpretation of protein adsorption on substrates functionalized by polyelectrolytes. Full article
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