MS-BIOE-L Archives

November 2020


Options: Use Proportional Font
Show HTML Part by Default
Condense Mail Headers

Message: [<< First] [< Prev] [Next >] [Last >>]
Topic: [<< First] [< Prev] [Next >] [Last >>]
Author: [<< First] [< Prev] [Next >] [Last >>]

Print Reply
multipart/alternative; boundary="_000_BL0PR05MB48193914AA9EC18C346CE2FD94EA0BL0PR05MB4819namp_"
Mon, 9 Nov 2020 19:53:39 +0000
Carol McHugh <[log in to unmask]>
Carol McHugh <[log in to unmask]>
MS-BIOE-L <[log in to unmask]>
text/plain (3293 bytes) , text/html (10 kB)
Notice and Invitation
Oral Defense of Master's Thesis
Bioengineering Department
The Volgenau School of Engineering, George Mason University

Luz Merlyn Vargas Restrepo

Bachelor of Science, Universidad de Antioquia, 2016

DNA Nanotechnology as a Tool to Study Membrane-binding Events:
The Role of RGD Peptide Spatial Organization on AVB3 Integrin binding

Monday, November 16, 2020, 2pm-4pm

via Zoom (link below)
All are invited to attend.

Dr. Parag Chitnis, Chair
Dr. Remi Veneziano, Thesis Director
Dr. Barney Bishop


Receptor-mediated recognition, interaction and entry into cells are fundamental mechanisms in cell biology notably for the control of cell fate and behavior. However, the role of specific spatial arrangements of biomolecules in the recognition and binding by receptors, as well as the kinetic parameters of these interactions for many biological mechanisms are not yet fully understood. For instance, mechanisms such as cell adhesion and migration are fundamental biological mechanisms for which the role of nanoscale organization of specific ligands responsible of the interactions with the extracellular matrix is still not clear. To date, extensive efforts have been made in using RGD peptide nanopatterns on surface to investigate specific adhesion of various cells and the subsequent proliferation, migration, and differentiation behaviors. However, despite years of research, the effect of the nanoscale organization of RGD peptide on the interaction with cell membrane receptors remains limited, mainly because of the lack of techniques that allow for nanoscale control of biomolecules organization and precise stoichiometry control.
In this work, we address this problem by developing DNA origami presenting RGD peptide systems. These multifunctional DNA origami nanoparticles were designed, folded and functionalized to explore the impact of spacing, and 1D vs 2D organization of RGD peptide on binding to Šv‚3 integrin at the single-protein level.
We show that binding affinity to Šv‚3 membrane receptor can be modulated by controlling RGD inter-peptide distance on DNA origami nanoparticles, using surface plasmon resonance (SPR). In conclusion, DNA origami-RGD peptide systems not only represent potential for helping elucidate the role of RGD and its organization in membrane binding interactions, but also to assemble the new generation of nanocarriers for drug delivery and effective scaffold for cell-tissue engineering.

Parag Chitnis is inviting you to a scheduled Zoom meeting.

Topic: MS Thesis Defense of Merlyn Vargas
Time: Nov 16, 2020 02:00 PM Eastern Time (US and Canada)

Join Zoom Meeting

Meeting ID: 960 8572 7766
Passcode: 748649
One tap mobile
+12678310333,,96085727766#,,,,,,0#,,748649# US (Philadelphia)
+13017158592,,96085727766#,,,,,,0#,,748649# US (Washington D.C)

Dial by your location
        +1 267 831 0333 US (Philadelphia)
        +1 301 715 8592 US (Washington D.C)
Meeting ID: 960 8572 7766
Passcode: 748649
Find your local number:

Join by SIP
[log in to unmask]<mailto:[log in to unmask]>

Carol McHugh
Academic Program Assistant
Department of Bioengineering
3100 Peterson Family Health Services Hall