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SUMMARY:Biofunctional DNA Nanotech Mini Symposium
DTSTART:20240826T140000
DTEND:20240826T160000
DTSTAMP:20260408T153235Z
UID:c8147047ffaf581f7b86d3e9e4713d5616083ebe6cd602ba15196470
CATEGORIES:Conferences - Seminars
DESCRIPTION:- PD Dr. Adrian Keller\, Dept. of Technical and Macromolecular
  Chemistry\, Paderborn University\, Paderborn (Germany)\n\n- Prof. Barbara
  Saccà\, Dept. of Bionanotechnology\, University of Duisburg-Essen\, Esse
 n (Germany)\nBiofunctional DNA Nanotech Mini Symposium - double talk semi
 nar\n \n\n[1] DNA Origami Nanostructures for Antimicrobial Therapy\n  
    PD Dr. Adrian Keller\, Dept. of Technical and Macromolecular Chemistr
 y\, Paderborn University\, Paderborn (Germany)\n\nAbstract:\nDNA origami h
 as become a widely employed method for synthesizing fully biocompatible\, 
 biodegradable\, and nontoxic nanocarriers for biomedicine. In this regard\
 , previous research has mostly focused on applications in cancer therapy\,
  whereas potential applications in the treatment and prevention of infecti
 ous diseases have only recently received broader attention.\nThis presenta
 tion will summarize our recent and ongoing activities directed at synthesi
 zing\, characterizing\, and testing antimicrobial DNA origami nanostructur
 es for combating drug-resistant bacteria. In particular\, we investigate a
 pplications of DNA origami nanostructures as nanocarriers in antimicrobial
  photodynamic therapy and as templates for the synthesis of multivalent an
 tibiotics nanoarrays with enhanced antimicrobial activity. Both approaches
  are tested against model bacteria and the most promising formulations are
  identified. Potential strategies for a further enhancement of antimicrobi
 al activity will be discussed.\n\n[2]  Modular DNA Origami Compartments f
 or the Engineering of a Protein Unfolding and Degradation Pathway\n   
    Prof. Barbara Saccà\, Dept. of Bionanotechnology\, University of Dui
 sburg-Essen\, Essen (Germany)\n\nWithin the cell\, chemical reactions are 
 often confined and organized through a modular architecture. This facilita
 tes the targeted localization of molecular species and their efficient tra
 nslocation to subsequent sites. Here\, we present a cell-free nanoscale mo
 del that exploits this compartmentalization principle to carry out regulat
 ed protein unfolding and degradation. Our model is composed of two connect
 ed DNA origami nanocompartments\, one containing the protein unfolding mac
 hine\, p97\, and the other housing the protease chymotrypsin. We achieve t
 he unidirectional immobilization of p97 within the first compartment\, est
 ablishing a ‘gateway’ mechanism that controls substrate recruitment\, 
 translocation\, and processing within the second compartment. Our data sho
 w that\, whereas spatial confinement increases the rate of the individual 
 reactions\, physical connection of the compartmentalized enzymes into a ch
 imera further improves their performance and minimizes off-target proteoly
 sis. We anticipate that our modular approach may serve as a blueprint for 
 engineering artificial nanofactories with reshaped catalytic performance a
 nd functionalities even beyond those observed in natural systems.
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717 https://epfl.zoom.u
 s/j/65694102711
STATUS:CONFIRMED
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