The 2nd International Electronic Conference on Biomolecules: Biomacromolecules and the Modern World Challenges
Part of the International Electronic Conference on Biomolecules series
1–15 Nov 2022
Proteins, Carbohydrates, Nucleic Acids, Lipids, Ecology, Health, Technology
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IECBM 2022 is closed. Thanks for your participation.
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See you in the next edition.
Welcome from the Chair
It is with great enthusiasm that we announce the 2nd International Electronic Conference on Biomolecules: Biomacromolecules and the Modern World Challenges (IECBM2022). The conference is organized by the MDPI open-access journal Biomolecules (Impact Factor 6.064), and will be held online from 1-15 November 2022.
This conference will 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 and sessions of the conference are:
Biomacromolecules: Nucleic Acids;
This online event will bring together researchers from all over the world with no concerns of travel or other related expenditures. Participation and “attendance” to the IECBM2022 are FREE of charge.
The conference invites submissions for abstracts that will be reviewed by the conference committee. The authors of accepted contributions will be invited to submit a conference paper along with a slide or poster presentation of their work. All participants will have the opportunity to examine, explore, and critically engage with research findings published in Sciforum during the conference.
After the conference, all accepted papers will be published in the proceedings of this e-conference within a dedicated issue of the MDPI journal Biology and Life Sciences Forum. In addition, all participants will be encouraged to submit a full paper to one dedicated Special Issue in Biomolecules with a 20% discount on the article processing charges (APC).
We hope that you will join this e-conference to exchange ideas, start fruitful collaborations, and make this edition a success.
Prof. Dr. Vladimir N. Uversky, PhD, DSc, FRSB, FRSC
List of accepted submissions (53)
|Id||Title||Authors||Presentation Video||Presentation Pdf|
Coaxial wet-spun fibers loaded with AAPV – a viable option for chronic wound healing
Submitted: 11 Mar 2022
Abstract: Show Abstract
Chronic wounds (CW) are a worldwide concern, causing serious strives on the health and quality of patients’ life. In CW, human neutrophil elastase (HNE) enzyme gets highly expressed during inflammation, reaching abnormally elevated concentrations. Additionally, prevalence of Staphylococcus aureus-induced infections remains very high and difficult to treat. Considering these phenomena, a drug delivery system made of co-axial wet-spun fibers, loaded with the tetrapeptide Ala-Ala-Pro-Val (AAPV, a known inhibitor of HNE activity) and N-carboxymethyl chitosan (NCMC, responsive to neutral-basic pH’s, characteristic of CW and endowed with antibacterial features), was proposed.
AAPV was synthesized by solid-phase peptide synthesis, whereas NCMC was synthesized from low molecular weight chitosan in a chloroacetic acid mixture. HNE inhibition tests were conducted to establish the AAPV IC50 in 1.50 µg/mL and the NCMC minimum bactericidal concentration (MBC) against S. aureus in 6.40 mg/mL. These determinations were used to establish fiber loading amounts. Core-shell structures were produced with 10% w/v polycaprolactone (PCL) at the core and 2% w/v sodium alginate (SA) solutions at the shell. NCMC was mixed with SA at 2xMBC so neutral-basic pH-triggered solubility (characteristic of CW) would allow pores to be opened in the outer layer for accessing the core, where AAPV was combined with PCL.
Fourier-transform infrared spectroscopy and brightfield microscopy were used to confirm the presence of the four components on the fibers and the co-axial architecture, respectively. Fibers presented maximum elongations of over 100%. Release kinetics studies conducted via UV-visible absorption spectroscopy mapped NCMC liberation overtime but were uncapable of detecting AAPV, since polymer degradation masked AAPV absorption peaks. Time-kill kinetics studies against S. aureus demonstrated the effectiveness of NCMC in eliminating this bacterium, particularly after 6 h of incubation. On its turn, AAPV guaranteed HNE inhibition. Data demonstrated the potential of SA-NCMC-PCL-AAPV co-axial systems to work as stepwise, pH-triggered delivery platforms.
Use of mango by-products in the development of functional confectionery
Submitted: 30 Mar 2022
Abstract: Show Abstract
The mango (Mangifera indica L.) is one of the most cultivated fruits in the world, however, its processing generates high amounts of waste, called agro-industrial by-products, among which the stone or seed, peel and bagasse stand out. It has been reported that these by-products contain significant amounts of nutrients and phytochemicals, mainly fiber and phenolic compounds, which represent a potential added value for the food industry, which has increased the interest in their study and applications by various authors. One of these booming applications is functional confectionery, which represents a vehicle for taking advantage of the benefits of these by-products. Therefore, the present work seeks to develop and evaluate the effect of a functional confectionery product (gummy) enriched with different concentrations of bagasse and mango peel on the texture profile characteristics (TPA), essential for sensory evaluation, selecting the mixture with greater similarity to the commercial product for its subsequent proximal characterization. As a result, for mixture 2, which contains a high pectin and bagasse content, added to a low shell content, with respect to the other mixtures, it presents a TPA profile similar to the control commercial gummy. The proximal composition showed 41% carbohydrates, of which 59% belongs to total dietary fiber, divided into 26% soluble and 33% insoluble. When performing the Pearson correlation of mixtures vs. the texture profile, the hardness parameter is negatively correlated with the type of mixture, which in turn is related to both the gumminess and the chewiness of the product. These results suggest that it is possible to incorporate these agro-industrial by-products into food and that it is comparable with that already marketed. In addition, with its high percentage of fiber, it could be considered a potentially prebiotic food.
Space and terrestrial temperature-induced nucleation and growth of protein single crystals
Submitted: 29 Jul 2022
Abstract: Show Abstract
A method is described for high-quality protein crystal solution growth with the help of localized action of a thermal control field. Two techniques for the nucleation and growth of single crystals of biological macromolecules have been proposed. The first one utilizes a very slow temperature shift at a capillary point where the crystal is to be grown. This allows to suppress an undesirable multiple nucleation. The second technique includes several local rapid temperature changes (a temperature “shock”) forcing the nucleation at the given point.
A mathematical model has been developed and computational investigation has been performed of the processes of protein crystallization from a homogeneous aqueous solution in the crystallization volume. The mathematical model describes crystal nucleation and growth depending on the local supersaturation and temperature as well as heat-and-mass exchange within the entire volume of the solution including the protein crystals.
The temperature was shown to be a factor, capable to initiate and drive the crystallization, and also to influence the nucleation stage and, hence, the protein crystal morphology. This may be useful for obtaining good quality single crystals of biological macromolecules. One or the other technique may be chosen. The stronger the dependence of protein solubility against the temperature, the better chances one has to succeed with any of the approaches, especially with the first one.
The mathematical model developed describes the process of nucleation and growth of protein crystals from solution under the control action of a thermal field based on an intermediate phase concept, the intermediate phase consisting of a mixture of solid and liquid phase fractions. This model was used to calculate an experiment on growing a protein crystal from a homogeneous aqueous solution, with the process of crystal nucleation and growth being acted upon by the precipitant and the thermal field. The calculations showed that this model is adequate to the processes being modeled and can be used for parametric investigations and predictive calculations of protein crystallization processes under thermal control field conditions both under terrestrial and space conditions.
These techniques were successfully tested while growing single crystals of lysozyme, xylanase and human serum albumin (HSA) respectively.
Structural and Conformational Dynamics of a Disordered Protein Motif
Submitted: 01 Apr 2022
Abstract: Show Abstract
SALS (sarcomere length short), a WH2-domain-containing protein was identified in Drosophila as an important regulator of the assembly of sarcomeric actin structures (Bai et al.(1)). It contributes to the establishment of sarcomere length and organization by promoting the lengthening of actin filaments at the pointed end. The absence of SALS is already lethal in the embryonic age. This may be due to the shortening of the length of sarcomeric actin filaments, and/or the disruption of their organization.
SALS is a relatively large protein, consisting of 935 amino acids. According to our bioinformatics analysis, it is an intrinsically disordered protein (IDP). IDPs are biologically active proteins, that, however, do not have a well-defined three-dimensional structure. They possess specific physicochemical properties, different from those of ordered proteins (e.g. hydrophilic/charged:hydrophobic amino acid ratio, thermal stability, electrophoretic mobility).
In the case of SALS previous studies have revealed only two motifs consisting of a few 10 amino acids, called Wiscott-Aldrich syndrome homology 2 (WH2) domains, that are intrinsically disordered protein regions (IDR) of low structural complexity. Considering their role, they possess actin-binding properties. Depending on the number and sequence of domains, proteins containing WH2 show multifunctional properties.
In our previous research we completed the functional analysis of the SALS WH2 domains (SALS-WH2) (2). Based on our results both of the SALS WH2 domains interact with the actin, and through their activities shift the monomer:filament ratio towards monomeric actin. We further aimed to characterize the structural and conformational dynamic properties of SALS-WH2 by using in silico and experimental approaches. Our bioinformatics analysis suggests that the SALS-WH2 domains have IDR elements. Our prediction-based results were experimentally verified by fluorescence spectroscopy and thermal analysis.
(1) Bai J, Hartwig JH, Perrimon N. SALS, a WH2-domain-containing protein, promotes sarcomeric actin filament elongation from pointed ends during Drosophila muscle growth. Dev Cell.2007 Dec;13(6):828-42.
(2) Tóth MÁ, Majoros AK, Vig AT, Migh E, Nyitrai M, Mihály J, Bugyi B. Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein. J Biol Chem. 2016 Jan 8;291(2):667-80.
New National Excellence Program of the Ministry for Innovation and Technology ÚNKP-21-3-II-PTE-997 (PG), University of Pécs, Medical School, KA-2021-30 (AV). We thank József Mihály (Institute of Genetics, Biological Research Centre) for the SALS plasmid.
pH-dependent specificity of papain-like cysteine proteases is determined by S1 binding pocket
Submitted: 31 Mar 2022
Abstract: Show Abstract
Papain-like cysteine proteases (PLCPs) are widely expressed enzymes, the main function of which is low-specific protein turnover in the acidic conditions of lysosomes. Additionally, these proteases provide specific functions in other compartments such as cytosol, nucleus, and extracellular space. The specificity of each protease to its substrates mainly depends on the patterns of the amino acids in the binding cleft. This specificity is highly regulated by media conditions and the presence of accessory proteins. In this study, we examined structural aspects ensuring pH-dependent substrate specificity of PLCPs. Experiments employing fluorogenic peptide substrates demonstrated that plant PLCPs and human cathepsins possess a pH-dependent specificity for the residue in the P1 position. X-ray crystallographic studies and molecular simulations allowed overall structure determination of the enzymes to predict residues in the S1 binding pocket which can form electrostatic contacts with the substrates. Sequence analysis established variability of these residues among PLCPs. Based on the obtained data we designed a peptide inhibitor for human cathepsin L and described its inhibitory potential. As a conclusion, we state that the S1 binding pocket defines specific pH-dependent recognition of substrates by PLCPs, ensuring multiple physiological functions of these proteases. This work was supported by the Russian Science Foundation (grant No. 22-25-00648).
Ms. Sienna Tian
Ms. Billie Jiao
Ms. Yufei Shi
Ms. Sara Wang
Ms. Letty Zhu
MDPI Branch Office, Beijing
E-mail: [email protected]
Department of Molecular Medicine, University of South Florida, USA
Vladimir Uversky is Professor at the College of Molecular Medicine, University of South Florida. He is a biophysicist and obtained his PhD and Doctor of Science (DSc) in Physics and Mathematics at the Moscow Institute of Physics and Technology (1991) and at the Institute Experimental and Theoretical Biophysics, Russian Academy of Sciences (1998), respectively. He spent his early career investigating protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, he moved to the University of California Santa Cruz to work on protein folding, misfolding, and protein intrinsic disorder. In 2004, he joined the Indiana School of Medicine and, in 2010, the University of South Florida, where he has since been continuing his studies on protein folding, misfolding, and intrinsically disordered proteins. Prof. Vladimir Uversky has authored over 980 scientific publications, edited numerous books, and is also serves as the editor of several scientific journals. He was included in Thomson Reuters list of Highly Cited Researchers in 2014-2020.
Research Director, ISOF, Consiglio Nazionale delle Ricerche, Italy
Interests: free radical chemistry; biomimetic chemistry; organic synthesis; reaction mechanism; analytical protocols for biomarkers of radical stress; oxidative DNA damage; lipid modification; fatty acid-based lipidomics
Laboratoire de Biologie des Ligneux et des Grandes Cultures (LBLGC), INRA USC1328, Université ď Orléans, France
Interests: chemistry of natural products; analytical methods; HPLC; LC-MS; polyphenols (lignans, flavonoids, phenolic acids); ethnopharmacology; history of pharmacy
Institute of Translational Medicine, Faculty of Health Sciences, University of Macau, China
Interests: novel therapeutic antibodies development; venom-based peptide & natural biomolecule prototype drugs development; cancer biomarkers & immunotherapy markers discovery for prognostic and therapeutic validation
School of Systems Biology and The Krasnow Institute for Advanced Study, George Mason University, USA
Interests: multiscale systems biology; computational biology; bioinformatics; cardiac physiology; immunology; mitochondria; cellular signaling; neuroscience; algorithms; HPC
Center for RNA Medicine, Department of Clinical Medicine, Aalborg University, Denmark
Interests: bioinformatics; cardiovascular system; circRNA; database; epitranscriptomics; lncRNA; miRNA; non-coding RNA
Department of Nutrition and Food Science, University of Granada, Campus of Cartuja, Spain
Interests: antioxidants; natural product chemistry; antioxidant activity; phytochemicals; lipids; lipid oxidation
Department of Biomedical and Molecular Sciences, Queen’s University, Kingston, ON K7L 3N6, Canada
Interests: immunology; COVID-19 and ACE2 receptor; cancer; inflammation; TLR receptor; Trk receptor; GPCR signaling; insulin receptor; glycosylation; NEU1 sialidase
CSIC Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Santander, Spain
Interests: RAS; ERK; MAP kinases; scaffold proteins; signalling spatial regulation
Department of Chemistry, University of Coimbra, 3004 - 535 Coimbra, Portugal
Interests: transport properties; thermodynamic properties; electrolytes; polyelectrolytes; polymers; carbohydrates; drugs; carriers; dental alloys; corrosion
Call for Abstracts
The 2nd International Electronic Conference on Biomolecules will be held from 1-15 November, 2022. IECBM aims to promote and advance the exciting and rapidly changing field of biomacromolecules and the modern world challenges. All abstracts and presentations will be held online at https://iecbm2022.sciforum.net/.
Topics of interest include, but are not limited to:
Biomacromolecules: Proteins (Session A);
Biomacromolecules: Carbohydrates (Session B);
Biomacromolecules: Nucleic Acids (Session C);
Biomolecules: Lipids (Session D).
The conference will be completely free of charge—both to attend and for scholars to upload and present their latest work on the conference platform. There will also be the possibility to submit selected papers to the journal Biomolecules ( ISSN: 2218-273X; Impact Factor: 6.064) with a 20% discount on the APCs.
IECBM 2022 offers you the opportunity to participate in this international, scholarly conference without having the concern or expenditure of travel—all you need is your computer and access to the Internet. We would like to invite you to “attend” this conference and present your latest work.
Abstracts (in English) should be submitted by 29 July 2022 online at https://iecbm2022.sciforum.net/. For accepted abstracts, the presentations can be submitted by 16 September 2022. The abstracts and presentations will be available on Sciforum for discussion during the time of the conference (1-15 November 2022) and will be then published in the Journal Biology and Life Sciences Forum.
We hope you will be able to join this exciting event and support us in making it a success. IECBM 2022 is organized and sponsored by MDPI, a scholarly open-access publisher based in Basel, Switzerland.
Instructions for Authors
Submissions should be made by authors online by registering with https://iecbm2022.sciforum.net/, and using the "New Submission" function once logged into the system.
- Scholars interested in participating in the conference can submit their abstract (about 200–300 words) online on this website until 29 July 2022.
- The Conference Committee will notify the acceptance of the abstract by 10 August 2022.
- If the abstract is accepted for this conference, the author will be invited to prepare a full description of their work in the form of a Poster/PowerPoint/Video Presentation (max. 5 minutes), until the submission deadline 9 September 2022. Authors will receive a notification about the acceptance of their presentations by 11 October 2022.
- The abstracts and presentations will be available on https://iecbm2022.sciforum.net/ for discussion and rating during the time of the conference, from 1-15 November 2022.
- All accepted abstracts+presentations will be published as one dedicated volume in MDPI Biology and Life Sciences Forum (ISSN: 2504-3900). Publication of the proceedings will be free of charge.
- The open-access journal Biomolecules (Impact Factor 6.064) will publish a conference Special Issue. Conference participants are encouraged to submit a full paper to the dedicated Special Issue and will receive a 20% discount on the Article Processing Charges (APC), in case their paper is accepted for publication after peer-review.
Submission of Manuscripts
Authors are encouraged to prepare a presentation in PowerPoint or similar software, to be displayed online along with the manuscript. Slides can be prepared the same way as for any traditional conference. They should be converted to PDF format before submission.
Authors are also encouraged to submit video presentations. This is an unique way of presenting your paper and discussing it with peers from all over the world. Video should be no longer than 5 minutes and prepared with one of the following formats: .mp4 / .webm / .ogg (max size: 250Mb). Videos should be submitted with a copy of the accepted abstract by 9 September 2022.
Posters will be available on this conference website during and after the event, participants will be able to ask questions and make comments about the posters. Authors that wish to present a poster must follow the following instructions: 1) The poster should be in PDF format; 2) The content of the poster should be a comprehensive presentation of your accepted submission; 3) No copyright issues with any elements in the poster. Posters should be submitted along with a copy of the accepted abstract by 9 September 2022.
All authors must disclose all relationships or interests that could inappropriately influence or bias their work. This should be conveyed in a separate "Conflict of Interest" statement preceding the "Acknowledgments" and "References" sections at the end of the manuscript. If there is no conflict, please state "The authors declare no conflict of interest." Financial support for the study must be fully disclosed under "Acknowledgments" section.
MDPI, the publisher of the Sciforum.net platform, is an open access publisher. We believe that authors should retain the copyright to their scholarly works. Hence, by submitting a communication paper to this conference, you retain the copyright of your paper, but you grant MDPI the non-exclusive right to publish this paper online on the Sciforum.net platform. This means you can easily submit your paper to any scientific journal at a later stage and transfer the copyright to its publisher (if required by that publisher).
The Sponsor Biomolecules offers one Best Contribution Award and one Best Poster Award to our participants.
Number of Awards Available: 1300 CHF + publication waiver in Biomolecules Journal
Number of Awards Available: 1300 CHF
Terms and Conditions:
All formats of presentations will be eligible for the Best Contribution Award.
- Originality / Novelty
- Significance of content
- Scientific soundness
- Interest to the readers
- English language and style
- Each Evaluation Committee member will assess the criteria outlined above for each application.
- Presentations will be ranked from highest to the lowest total score.
- If two or more authors get the same score, further evaluation will be carried out.
- Winners will be announced online after the conference.
A. Biomacromolecules: Proteins
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B. Biomacromolecules: Carbohydrates
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C. Biomacromolecules: Nucleic Acids
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D. Biomolecules: Lipids
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