[Todos] Recordatorio: Invitación al Seminario Conjunto INIFTA – IFLP. Título: "Nanopores: Protein Confinement” a cargo del Prof. Dr. Igal Szleifer. Universidad de Northwestern. EE.UU.

[Claudia Rodríguez Torres]

Recordatorio seminario conjunto INIFTA-IFLP mañana:

--------------------------------------------------------------------------



Quedan todas/os invitadas/os al próximo seminario a realizarse el *viernes
25 de octubre a las 11hs*.



El mismo estará a cargo del *Prof. Dr. Igal Szleifer. *Departamentos de
Ingeniería Biomédica, Química y Medicina. Universidad de Northwestern.
EE.UU.



Su charla se titula:


*"Nanopores: Protein Confinement"*



Se envía a continuación un breve resumen:


1)           How Does Confinement Change Ligand−Receptor Binding
Equilibrium? Protein Binding in Nanopores and Nanochannels



We present systematic studies for the binding of small model proteins to
ligands attached to the inner walls of long nanochannels and short
nanopores by polymeric tethers. Binding of proteins to specific ligands
inside nanometric channels and pores leads to changes in their ionic
conductance, which have been exploited in sensors that quantify the
concentration of the proteins in solution. The theoretical predictions
presented in this work are aimed to provide a fundamental understanding of
protein binding under geometrically confined environments and to guide the
design of this kind of nanochannel-based sensors. The theory predicts that
the fraction of the channel volume filled by bound proteins is a
nonmonotonic function of the channel radius, the length of the tethers, the
surface density of the ligands and the size of the proteins.



2)           Orientational Pathways during Protein Translocation through
Polymer-Modified Nanopores



Protein translocation through nanopores holds significant promise for
applications in biotechnology, biomolecular analysis, and medicine.
However, the interpretation of signals generated by the translocation of
the protein remains challenging. In this way, it is crucial to gain a
comprehensive understanding on how macromolecules translocate through a
nanopore and to identify what are the critical parameters that govern the
process. In this study, we investigate the interplay between protein charge
regulation, orientation, and nanopore surface modifications using a
theoretical framework that allows us to explicitly take into account the
acid−base reactions of the titrable amino acids in the proteins and in the
polyelectrolytes grafted to the nanopore surface. Our goal is to thoroughly
characterize the translocation process of different proteins (GFP, β-
lactoglobulin, lysozyme, and RNase) through nanopores modified with weak
polyacids. Our calculations show that the charge regulation mechanism
exerts a profound effect on the translocation process. The pH-dependent
interactions between proteins and charged polymers within the nanopore lead
to diverse free energy landscapes with barriers, wells, and flat regions
dictating translocation efficiency. Comparison of different proteins allows
us to identify the significance of protein isoelectric point, size, and
morphology in the translocation behavior. Taking advantage of these
insights, we propose pH responsive nanopores that can load proteins at one
pH and release them at another, offering opportunities for controlled
protein delivery, separation, and sensing applications.



El evento tendrá lugar en el *auditorio ¨Prof. Dr. Luis N. Epele¨ del IFLP*,
sito en la diagonal 113 entre 63 y 64.



Adjuntamos también flyer del evento del cual agradeceremos su difusión.



Esperamos contar con su presencia.



Saludos cordiales,



*Dra. Ángela M. Candreva*

*Secretaría Científica y de Vinculación*

*Instituto de Física La Plata (IFLP – UNLP - CONICET).*

*Diag. 113 e 63 y 64 s/n. La Plata - Bs. As. – Argentina.*

*e-mail: **acandreva at iflp.unlp.edu.ar* <acandreva at iflp.unlp.edu.ar>

_______________________________________________
Iflpinvestigadores mailing list
Iflpinvestigadores at fisica.unlp.edu.ar
http://mail.fisica.unlp.edu.ar/cgi-bin/mailman/listinfo/iflpinvestigadores
-------------- next part --------------
An HTML attachment was scrubbed...
URL: <http://mail.fisica.unlp.edu.ar/pipermail/todos/attachments/20241024/035da610/attachment-0001.html>
-------------- next part --------------
A non-text attachment was scrubbed...
Name: Seminario Igal Szleifer.jpg
Type: image/jpeg
Size: 81004 bytes
Desc: not available
URL: <http://mail.fisica.unlp.edu.ar/pipermail/todos/attachments/20241024/035da610/attachment-0001.jpg>