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First Canadian Peptide and Protein Community Virtual Symposium

27/05/2021 - 28/05/2021
Abstract Submission
22nd April 2021
Acceptance Notification
28th April 2021
File Submission
10th May 2021

Proteins, Peptide Science, Medicinal Chemistry
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Welcome from the Chairs

Peptides and proteins are remarkable natural biopolymers, which inspire various fields of contemporary research. Moreover, they serve as components of a variety of medicines, catalysts, materials, cosmetics, and agricultural products. Our virtual symposium brings together leading researchers at the cutting edge of peptide and protein science. With a broad focus and the intent to promote the visibility of emerging scientists and young investigators, this two-day event will feature leaders in the characterization, synthesis, and application of peptides and proteins in various domains that have been targeted to improve our basic knowledge and to enhance our quality of life.

Conference Secretariat
Mr. Vincent Pang
Ms. Betsy Feng
Ms. Celia Xu

email: [email protected]

Conference Chairs

Professor William Lubell

Département de chimie, Université de Montréal

Professor Éric Biron

Faculty of Pharmacy, Université Laval and Centre de recherche du CHU de Québec

Professor Voula Kanelis

Department of Chemical and Physical Sciences, University of Toronto Mississauga, and Departments of Chemistry and Cell & Systems Biology, University of Toronto

Professor Leonard G. Luyt

Western University Sr. Scientist, London Regional Cancer Program

Professor David Perrin

Department of Chemistry, University of British Columbia

Professor Jumi Shin

Department of Chemistry, University of Toronto

Invited Speakers

Professor Marya Ahmed

Department of Chemistry and Faculty of Sustainable Design Engineering, University of Prince Edward Island

DETAILS

Title: Stimuli Responsive, Antimicrobial and Immunomodulatory Properties of Peptide Based Materials

Antimicrobial peptides are a diverse class of cationic and amphipathic peptides that display a broad-spectrum antimicrobial activity against gram positive and gram-negative bacteria and play a key role in innate immunity of multicellular organisms. With growing concerns over the development of antibiotic resistance microbial strains, antimicrobial peptides are much studied alternative in research. This talk mainly focuses on the synthesis of chimeric peptides, and their nanoparticles and evaluation of their antimicrobial and anti-inflammatory properties. The synthesis of peptides-based materials (polymer peptide hybrids and microparticles) and their role as stimuli responsive and drug delivery carriers will also be discussed.

Talk
Title: Stimuli Responsive, Antimicrobial and Immunomodulatory Properties of Peptide Based Materials
Bio
Antimicrobial peptides are a diverse class of cationic and amphipathic peptides that display a broad-spectrum antimicrobial activity against gram positive and gram-negative bacteria and play a key role in innate immunity of multicellular organisms. With growing concerns over the development of antibiotic resistance microbial strains, antimicrobial peptides are much studied alternative in research. This talk mainly focuses on the synthesis of chimeric peptides, and their nanoparticles and evaluation of their antimicrobial and anti-inflammatory properties. The synthesis of peptides-based materials (polymer peptide hybrids and microparticles) and their role as stimuli responsive and drug delivery carriers will also be discussed.

Professor Steve Bourgault

Department of Chemistry, Université du Québec à Montréal, Montreal, Canada

DETAILS

Title: Peptide-based amyloid nanostructures: from mechanisms of self-assembly to synthetic nanovaccines

Endogenous proteins are known for their ability to self-associate in living organisms into supramolecular structures that perform key physiological functions. Over the last two decades, amyloid fibrils that accomplish essential biological activities have been identified in almost all species, from bacteria to mammals. Amyloids are organized proteinaceous assemblies characterized by a cross-beta-sheet quaternary structure. The physico-chemical and biological properties of amyloids suggest that they hold great potential as biomaterials for medical applications. However, the usage of amyloids is still today limited by a number of issues, which include; (i) incomplete understanding of the mechanisms of self-assembly, (ii) challenge of controlling aggregation and self-assembly, (iii) difficulty of predicting the final supramolecular architecture from the primary sequence and (iv) potential toxicity of conformational intermediates. In this context, our research group aims at developing (bio)chemical approaches to control amyloid assembly and design functionalized peptide-based nanostructures. By using the islet amyloid polypeptide, whose deposition in the pancreatic islets is associated with type II diabetes, we are investigating the early steps of amyloidogenesis and the relation between quaternary structure and cellular toxicity. Besides, we are developing chemical strategies to modulate the (supra)molecular architecture of peptide assemblies in order to design novel synthetic nanovaccines against influenza.

Talk
Title: Peptide-based amyloid nanostructures: from mechanisms of self-assembly to synthetic nanovaccines
Bio
Endogenous proteins are known for their ability to self-associate in living organisms into supramolecular structures that perform key physiological functions. Over the last two decades, amyloid fibrils that accomplish essential biological activities have been identified in almost all species, from bacteria to mammals. Amyloids are organized proteinaceous assemblies characterized by a cross-beta-sheet quaternary structure. The physico-chemical and biological properties of amyloids suggest that they hold great potential as biomaterials for medical applications. However, the usage of amyloids is still today limited by a number of issues, which include; (i) incomplete understanding of the mechanisms of self-assembly, (ii) challenge of controlling aggregation and self-assembly, (iii) difficulty of predicting the final supramolecular architecture from the primary sequence and (iv) potential toxicity of conformational intermediates. In this context, our research group aims at developing (bio)chemical approaches to control amyloid assembly and design functionalized peptide-based nanostructures. By using the islet amyloid polypeptide, whose deposition in the pancreatic islets is associated with type II diabetes, we are investigating the early steps of amyloidogenesis and the relation between quaternary structure and cellular toxicity. Besides, we are developing chemical strategies to modulate the (supra)molecular architecture of peptide assemblies in order to design novel synthetic nanovaccines against influenza.

Professor Deniz Meneksedag Erol

Department of Chemical and Materials Engineering, Concordia University, Montreal, QC, Canada

DETAILS

Title: Cancer Activating Mutation in STAT5B: Elucidating the Impact on Protein Structure and Dynamics Using Atomistic Molecular Simulations

The STAT (signal transducer and activator of transcription) protein family is an important therapeutic target in leukemia and lymphoma. However, the lack of structural and dynamic information on STAT proteins limit drug design efforts. Two cancer activating mutations located in the SH2 domain of STAT5B, N642H and Y665F, are observed clinically and the molecular basis for their increased oncogenicity is not currently known. Additionally, patients with the N642H mutation are reported to have increased drug resistance and poor response to chemotherapy [1]. Here, we used molecular dynamics simulations to elucidate the dynamics of the wild type and oncogenic mutants of human STAT5B protein, and to provide a molecular basis for the increased oncogenicity. We carried out extensive atomistic simulations of the wild type and mutant STAT5B proteins. The N642H mutation (i) led to a more rigid SH2 domain; (ii) significantly affected the size and dynamics of the peptide binding pockets; and (iii) increased the intra-SH2 domain interactions. Analysis of the impact of the Y665F mutation on the SH2 domain will identify the shared or different characteristics of the two mutations. The structural and dynamic information uncovered in this work may facilitate the design of small molecule drugs targeting the cancer activating mutants of STAT5B.

Talk
Title: Cancer Activating Mutation in STAT5B: Elucidating the Impact on Protein Structure and Dynamics Using Atomistic Molecular Simulations
Bio
The STAT (signal transducer and activator of transcription) protein family is an important therapeutic target in leukemia and lymphoma. However, the lack of structural and dynamic information on STAT proteins limit drug design efforts. Two cancer activating mutations located in the SH2 domain of STAT5B, N642H and Y665F, are observed clinically and the molecular basis for their increased oncogenicity is not currently known. Additionally, patients with the N642H mutation are reported to have increased drug resistance and poor response to chemotherapy [1]. Here, we used molecular dynamics simulations to elucidate the dynamics of the wild type and oncogenic mutants of human STAT5B protein, and to provide a molecular basis for the increased oncogenicity. We carried out extensive atomistic simulations of the wild type and mutant STAT5B proteins. The N642H mutation (i) led to a more rigid SH2 domain; (ii) significantly affected the size and dynamics of the peptide binding pockets; and (iii) increased the intra-SH2 domain interactions. Analysis of the impact of the Y665F mutation on the SH2 domain will identify the shared or different characteristics of the two mutations. The structural and dynamic information uncovered in this work may facilitate the design of small molecule drugs targeting the cancer activating mutants of STAT5B.

Professor Voula Kanelis

Department of Chemical and Physical Sciences, University of Toronto Mississauga,
Departments of Chemistry and Cell & Systems Biology, University of Toronto

DETAILS

Title: The effect of regulatory interactions and disease mutations in the NBDs of SUR proteins, the regulatory subunits of K(ATP) channels

ATP sensitive potassium (KATP) channels are found in the pancreas, brain, and cardiovascular system. KATP channels are of vast medical importance, as mutations in K-ATP channels causes cardiovascular disease, neonatal diabetes, hyperinsulinism, or epilepsy. KATP channels consist of four pore-forming Kir6.2 proteins and four regulatory sulphonylurea receptor (SUR) proteins. Recent high-resolution structures of the pancreatic KATP channel provide insights into the mechanism of pore closing, but not pore opening, which involves MgATP binding and hydrolysis at the nucleotide binding domains (NBDs). Further, structural information is lacking for some of the regulatory regions in the SUR protein, which are also sites of disease-causing mutations and/or phosphorylation that regulate channel opening. Thus, additional structural studies are necessary to determine how the action of the NBDs regulates channel gating and the molecular basis by which mutations cause diseases. Using nuclear magnetic resonance, CD, and fluorescence spectroscopies, we have characterized structural changes in the SUR NBDs and regulatory regions imparted by disease-causing mutations and/or phosphorylation. Phosphorylation alters the structure of a regulatory linker and its interactions with the NBDs. NBDs bearing disease-causing mutations have altered binding to the membrane-spanning domains, even when the disease-causing mutation is not at the NBD/membrane domain interface, suggesting that mutations likely disrupt allosteric pathways linking the action of the NBDs to the membranespanning domains and ultimately KATP channel opening. Thus, our data shed light on the underlying molecular basis by which KATP channels are regulated by phosphorylation and how several SUR mutations cause disease.

Talk
Title: The effect of regulatory interactions and disease mutations in the NBDs of SUR proteins, the regulatory subunits of K(ATP) channels
Bio
ATP sensitive potassium (KATP) channels are found in the pancreas, brain, and cardiovascular system. KATP channels are of vast medical importance, as mutations in K-ATP channels causes cardiovascular disease, neonatal diabetes, hyperinsulinism, or epilepsy. KATP channels consist of four pore-forming Kir6.2 proteins and four regulatory sulphonylurea receptor (SUR) proteins. Recent high-resolution structures of the pancreatic KATP channel provide insights into the mechanism of pore closing, but not pore opening, which involves MgATP binding and hydrolysis at the nucleotide binding domains (NBDs). Further, structural information is lacking for some of the regulatory regions in the SUR protein, which are also sites of disease-causing mutations and/or phosphorylation that regulate channel opening. Thus, additional structural studies are necessary to determine how the action of the NBDs regulates channel gating and the molecular basis by which mutations cause diseases. Using nuclear magnetic resonance, CD, and fluorescence spectroscopies, we have characterized structural changes in the SUR NBDs and regulatory regions imparted by disease-causing mutations and/or phosphorylation. Phosphorylation alters the structure of a regulatory linker and its interactions with the NBDs. NBDs bearing disease-causing mutations have altered binding to the membrane-spanning domains, even when the disease-causing mutation is not at the NBD/membrane domain interface, suggesting that mutations likely disrupt allosteric pathways linking the action of the NBDs to the membranespanning domains and ultimately KATP channel opening. Thus, our data shed light on the underlying molecular basis by which KATP channels are regulated by phosphorylation and how several SUR mutations cause disease.

Professor Galia Maayan

Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa, Israel

DETAILS

Title: Peptoids as Versatile, Efficient and Selective Bio-Inspired Catalysts

Enzymatic catalysis is largely based on cooperativity between an active center and functional organic molecules located at its surrounding folds. High efficiency and selectivity are attributed to catalytic pockets within the structure of the proteins. Inspired by this concept, we design peptoid-based intramolecular catalytic systems in which the catalyst(s) and non-catalytic functional or structural groups are tethered in close proximity to each other, leading to highly efficient and/or selective catalytic systems for various important transformations. Peptoids, N-substituted glycine oligomers, can be efficiently generated by a solid-phase method that enables the incorporation of innumerable functional groups at specified N-positions along their spine, are stable towards different pH and oxidative conditions, and thus should be inert to catalytic transformations. In my talk I will demonstrate that peptoids can be used to facilitate cooperativity between several groups placed on one scaffold. I will show how we utilized this approach to design peptoids that catalyze (i) the oxidation of various benzylic, allylic and less activated aliphatic primary alcohols,1 (ii) the oxidative coupling of such alcohols with amines2,3 and (iii) the electrochemical oxidation of water,4,5 all with high conversions and low catalyst loadings via intramolecular cooperativity. I will also describe the cooperativity between non-selective catalysts embedded within peptoid sequences and the secondary structure of these peptoids and show how careful design of structure-function relationships leads to peptoids that catalyze (i) the oxidative kinetic resolution of alcohols,6 and (ii) the Michael addition reaction,7 both with high enentioselectivity.

Talk
Title: Peptoids as Versatile, Efficient and Selective Bio-Inspired Catalysts
Bio
Enzymatic catalysis is largely based on cooperativity between an active center and functional organic molecules located at its surrounding folds. High efficiency and selectivity are attributed to catalytic pockets within the structure of the proteins. Inspired by this concept, we design peptoid-based intramolecular catalytic systems in which the catalyst(s) and non-catalytic functional or structural groups are tethered in close proximity to each other, leading to highly efficient and/or selective catalytic systems for various important transformations. Peptoids, N-substituted glycine oligomers, can be efficiently generated by a solid-phase method that enables the incorporation of innumerable functional groups at specified N-positions along their spine, are stable towards different pH and oxidative conditions, and thus should be inert to catalytic transformations. In my talk I will demonstrate that peptoids can be used to facilitate cooperativity between several groups placed on one scaffold. I will show how we utilized this approach to design peptoids that catalyze (i) the oxidation of various benzylic, allylic and less activated aliphatic primary alcohols,1 (ii) the oxidative coupling of such alcohols with amines2,3 and (iii) the electrochemical oxidation of water,4,5 all with high conversions and low catalyst loadings via intramolecular cooperativity. I will also describe the cooperativity between non-selective catalysts embedded within peptoid sequences and the secondary structure of these peptoids and show how careful design of structure-function relationships leads to peptoids that catalyze (i) the oxidative kinetic resolution of alcohols,6 and (ii) the Michael addition reaction,7 both with high enentioselectivity.

Dr. Kevin McDonnell

Bicycle Therapeutics

DETAILS

Title: Tumor targeted Immune Cell Agonists (TICAs™) are fully synthetic, modular and tunable anti-cancer peptide therapeutics

Bicycles® are bicyclic peptides constrained via a chemical scaffold, which confers structural stability leading to high affinity and selectivity. Using phage display Bicycles have been discovered to both tumor cell and immune cell targets and using synthetic chemistry have been affinity optimized and assembled in a modular fashion to generate tumor targeted immune cell agonists (TICAsTM). These bispecific engagers simultaneously bind to overexpressed cell-surface targets on tumor cells (e.g. EphA2 or Nectin-4) and costimulatory receptors on immune cells (e.g. CD137 and OX40). This interaction leads to highly precise activation of immune cells in vitro, only in the presence of target positive tumor cells, and results in the secretion of pro-inflammatory cytokine such as IL2 and IFNg. In vivo, dosing of TICAs activates immune cells in the tumors of mice, resulting in potent anti-cancer immunity despite relatively short plasma exposures. TICAs represent a new generation of fully synthetic peptide-based immune modulatory anti-cancer agents.

Talk
Title: Tumor targeted Immune Cell Agonists (TICAs™) are fully synthetic, modular and tunable anti-cancer peptide therapeutics
Bio
Bicycles® are bicyclic peptides constrained via a chemical scaffold, which confers structural stability leading to high affinity and selectivity. Using phage display Bicycles have been discovered to both tumor cell and immune cell targets and using synthetic chemistry have been affinity optimized and assembled in a modular fashion to generate tumor targeted immune cell agonists (TICAsTM). These bispecific engagers simultaneously bind to overexpressed cell-surface targets on tumor cells (e.g. EphA2 or Nectin-4) and costimulatory receptors on immune cells (e.g. CD137 and OX40). This interaction leads to highly precise activation of immune cells in vitro, only in the presence of target positive tumor cells, and results in the secretion of pro-inflammatory cytokine such as IL2 and IFNg. In vivo, dosing of TICAs activates immune cells in the tumors of mice, resulting in potent anti-cancer immunity despite relatively short plasma exposures. TICAs represent a new generation of fully synthetic peptide-based immune modulatory anti-cancer agents.

Professor Caroline Proulx

Department of Chemistry, North Carolina State University

DETAILS

Title: Peptide ligations from tunable N-aryl peptide precursors

Chemoselective reactions that occur under mild conditions are required to synthesize and probe biomolecules in aqueous settings. To that end, ligation of -nucleophiles with -oxo-aldehydes or ketones have been pursued; however, addition of superstoichiometric amounts of aniline are typically required to construct oxime and hydrazone bonds at neutral pH via formation of an aniline Schiff-base intermediate. Moreover, while starting from ketone substrates instead of aldehydes would allow substitution at the site of ligation, synthetic challenges to access ketone derivatives from common amino acid building blocks and their slow reactivity in condensation reactions have precluded their widespread use in peptide ligations. Here, we expand the utility of oxime and hydrazone ligation reactions by providing direct access to reactive -imino amide intermediates from a site-selective, aerobic oxidation of N-aryl peptides. We demonstrate that the reactivity of N-aryl peptides can be modulated by the electronics of the aryl ring, and that various substitution at the -carbon can be introduced at the site of ligation in high yield. Efforts towards streamlining N-aryl peptide synthesis, as well as controlling E/Z ratios in ketoxime and kethydrazone peptides will also be discussed.

Talk
Title: Peptide ligations from tunable N-aryl peptide precursors
Bio
Chemoselective reactions that occur under mild conditions are required to synthesize and probe biomolecules in aqueous settings. To that end, ligation of -nucleophiles with -oxo-aldehydes or ketones have been pursued; however, addition of superstoichiometric amounts of aniline are typically required to construct oxime and hydrazone bonds at neutral pH via formation of an aniline Schiff-base intermediate. Moreover, while starting from ketone substrates instead of aldehydes would allow substitution at the site of ligation, synthetic challenges to access ketone derivatives from common amino acid building blocks and their slow reactivity in condensation reactions have precluded their widespread use in peptide ligations. Here, we expand the utility of oxime and hydrazone ligation reactions by providing direct access to reactive -imino amide intermediates from a site-selective, aerobic oxidation of N-aryl peptides. We demonstrate that the reactivity of N-aryl peptides can be modulated by the electronics of the aryl ring, and that various substitution at the -carbon can be introduced at the site of ligation in high yield. Efforts towards streamlining N-aryl peptide synthesis, as well as controlling E/Z ratios in ketoxime and kethydrazone peptides will also be discussed.

Professor Alanna Schepartz

Department of Chemistry, University of California Berkeley

DETAILS

Title: Coiled coil control of EGFR trafficking, signaling, lifetime, and cell fate

EGFR exhibits biased signaling, whereby growth factor or mutation-dependent changes in receptor conformation and/or dynamics elicit distinct intracellular outcomes. We report that many intracellular EGFR outcomes are controlled by a two-state coiled coil switch located within the juxtamembrane segment (JM), an essential component of the cytosolic dimer interface. The position of this switch defines the path of endocytic trafficking, the extent and dynamics of autophosphorylation, c-Cbl recruitment, and ubiquitination, and whether or not EGFR is degraded within lysosomes. It also predicts kinase-independent effects of oncogenic mutations and clinically relevant tyrosine kinase inhibitors (TKIs) that promote lysosome-based degradation. These findings provide a model for biased EGFR signaling, insights into kinase-independent activities of EGFR and clinically relevant TKIs, and identify new strategies for modulating protein lifetime.

Talk
Title: Coiled coil control of EGFR trafficking, signaling, lifetime, and cell fate
Bio
EGFR exhibits biased signaling, whereby growth factor or mutation-dependent changes in receptor conformation and/or dynamics elicit distinct intracellular outcomes. We report that many intracellular EGFR outcomes are controlled by a two-state coiled coil switch located within the juxtamembrane segment (JM), an essential component of the cytosolic dimer interface. The position of this switch defines the path of endocytic trafficking, the extent and dynamics of autophosphorylation, c-Cbl recruitment, and ubiquitination, and whether or not EGFR is degraded within lysosomes. It also predicts kinase-independent effects of oncogenic mutations and clinically relevant tyrosine kinase inhibitors (TKIs) that promote lysosome-based degradation. These findings provide a model for biased EGFR signaling, insights into kinase-independent activities of EGFR and clinically relevant TKIs, and identify new strategies for modulating protein lifetime.

Professor Suzana K. Straus

Department of Chemistry, University of British Columbia

DETAILS

Title: Strategies to Mitigate Host Defense Peptide (HDP) Toxicity

Host defense peptides (HDPs) have been the subject of great interest for the treatment of multidrug resistant bacterial infection due to their multimodal activity and low induction of resistance. However, concerns regarding aggregation, toxicity and short biological half-life have limited their applicability for clinical treatment. Many methods have been explored to improve these characteristics, such as polymer (e.g., polyethylene glycol (PEG) or hyperbranched polyglycerol (HPG)) conjugation, but these are often accompanied by reductions in the activity of the HDP. Here, we detail the design of novel conjugates with improved biocompatibility. In addition, a novel conjugate that incorporates an enzymatic cleavage sequence targeting matrix metalloproteinases (MMPs) that accumulate at sites of inflammation and infection will be presented.

Talk
Title: Strategies to Mitigate Host Defense Peptide (HDP) Toxicity
Bio
Host defense peptides (HDPs) have been the subject of great interest for the treatment of multidrug resistant bacterial infection due to their multimodal activity and low induction of resistance. However, concerns regarding aggregation, toxicity and short biological half-life have limited their applicability for clinical treatment. Many methods have been explored to improve these characteristics, such as polymer (e.g., polyethylene glycol (PEG) or hyperbranched polyglycerol (HPG)) conjugation, but these are often accompanied by reductions in the activity of the HDP. Here, we detail the design of novel conjugates with improved biocompatibility. In addition, a novel conjugate that incorporates an enzymatic cleavage sequence targeting matrix metalloproteinases (MMPs) that accumulate at sites of inflammation and infection will be presented.

Live Seesion

Date: 27-28 May 2021

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Instructions for Authors

Submission

Registration for this conference is FREE.

Submissions will be accepted online. Authors may submit their work by registering at www.sciforum.net and using the "Start New Submission" function once they are logged into the system. Please make other comments about contributing author’s status: post-doc, graduate student, or other in the process of submission.

  1. Scholars interested in participating in the conference can submit their abstract (200-word limit) on this website until 22 April 2021.
  2. The Chairs will pre-evaluate, based on the submitted abstract, whether a contribution will be included in the First Canadian Peptide and Protein Community Virtual Symposium. Authors will be notified by 28 April 2021 about the acceptance decision regarding their abstract.
  3. If the abstract is accepted, the author will be invited to prepare a PPT (oral presentation) or poster presentation by the submission deadline of 10 May 2021.

The open access journal Biomedicines will publish a Special Issue on the conference. After the conference, authors can submit the full papers to the aforementioned Special Issue (the submissions process will follow the usual procedure of the journal, including peer review, APC, etc.).

Presentation Slides

Authors are encouraged to prepare a presentation in PowerPoint or similar software, to be displayed online along with the manuscript. Slides, if available, will be directly displayed on the website using Sciforum.net’s proprietary slides viewer. Slides can be prepared in exactly the same way as for any traditional conference where research results can be presented. Slides should be converted to the PDF format before submission so that our process can easily and automatically convert them for online displaying.

CPPC oral presentation ppt template.pptx

Presentation of Posters

Posters will be available on this website during and after the event. As with papers presented at conferences, participants will be able to ask questions and make comments about the posters. Posters will be available online on this website during and after the virtual conference.

Posters should include the following:

    • Title (with authors and affiliations);
    • Introduction/objectives/aims;
    • Methods;
    • Results;
    • Conclusion;
    • References;
    • Acknowledgments;
    • Contact information.

    Potential Conflicts of Interest

    It is the authors’ responsibility to identify and declare any personal circumstances or interests that may be perceived as inappropriately influencing the representation or interpretation of clinical research. If there are no conflicts, please state here “The authors declare no conflicts of interest”. This should be conveyed in a separate “Conflicts of Interest” statement preceding the “Acknowledgments” and “References” sections at the end of the manuscript. Financial support for the study must be fully disclosed under the “Acknowledgments” section.

    Copyright

    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 an abstarct/poster or other files 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).

    Conference Awards

    To acknowledge the support of the conference’s esteemed authors and recognize their outstanding scientific accomplishments in the field of biomolecular and molecular science, we are pleased to launch the Best Oral Presentation Awards and the Best Poster Presentation Awards, sponsored by Biomedicines and International Journal of Molecular Sciences. Eight winners will be selected, and each winner will receive a cash award of USD 100. Winners will be announced at the end of the live session.

    The Awards
    Best Oral Presentation Awards
    The prize for each of the awards will consist of USD 100 (two will be awarded to graduate students and two to post-doctoral fellows).
    Best Poster Presentation Awards
    The prize for each of the awards will consist of USD 100 (two will be awarded to graduate students and two to post-doctoral fellows).
    Terms and Conditions:
    1. If the short abstract is accepted, PPT or posters must be submitted.
    2. Originality / Novelty of the paper
    3. Significance of Content
    4. Scientific Soundness
    5. Interest to the readers
    6. English language and style

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