Priscilla Do
University of Notre Dame
4 Papers
40 Citations
Priscilla Do is an academic researcher from University of Notre Dame. The author has contributed to research in topics: Major histocompatibility complex & T-cell receptor. The author has an hindex of 4, co-authored 4 publications.
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Papers
Fluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing manner
Kurt H. Piepenbrink,Oleg Y. Borbulevych,Ruth F. Sommese,John R. Clemens,Kathryn M. Armstrong,Clare Desmond,Priscilla Do,Brian M. Baker +7 more
TL;DR: Peptide fluorination provides a means to selectively modulate TCR binding affinity without significantly perturbing peptide composition or structure, and the results were most consistent with a 'polar hydrophobicity' mechanism, rather than a purely hydrophobic- or electrostatic-based mechanism.
Design, synthesis and evaluation of β-lactam antigenic peptide hybrids; unusual opening of the β-lactam ring in acidic media
Marion Tarbe,Itxaso Azcune,Eva Balentová,John J. Miles,Emily E. Edwards,Kim M. Miles,Priscilla Do,Brian M. Baker,Andrew K. Sewell,Jesus M. Aizpurua,Céline Douat-Casassus,Stéphane Quideau +11 more
TL;DR: None of the closed β-lactam peptides bound to HLA-A2, but their opened variants were shown to be moderate to good HLA -A2 ligands, one of them being even capable of stimulating a Melan-A-specific T cell line.
Engineering the Binding Properties of the T Cell Receptor:Peptide:MHC Ternary Complex that Governs T Cell Activity
Natalie A. Bowerman,Terence S. Crofts,Lukasz K. Chlewicki,Priscilla Do,Brian M. Baker,K. Christopher Garcia,K. Christopher Garcia,David M. Kranz +7 more
TL;DR: It is shown that a peptide substitution of QL9 (F5R), increased the affinity and stability of the pep-L(d) complex and provided a guide to designing the explicit binding parameters that govern optimal T cell activities.
Structures of native and affinity-enhanced WT1 epitopes bound to HLA-A*0201: Implications for WT1-based cancer therapeutics.
TL;DR: Stability measurements revealed how the R1Y substitution enhances MHC binding affinity, and together with the structures suggest a strategy for engineering WT1 variants with improved MHCbinding that retain the structural features of the native peptide/MHC complex.