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Beta-peptides as inhibitors of prote...

Kritzer, Joshua Aaron.

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Beta-peptides as inhibitors of protein-protein interactions.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Beta-peptides as inhibitors of protein-protein interactions./
作者:	Kritzer, Joshua Aaron.
面頁冊數:	173 p.
附註:	Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5856.
Contained By:	Dissertation Abstracts International66-11B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3194674
ISBN:	9780542394393

Beta-peptides as inhibitors of protein-protein interactions.
Kritzer, Joshua Aaron.

Beta-peptides as inhibitors of protein-protein interactions. - 173 p.

Source: Dissertation Abstracts International, Volume: 66-11, Section: B, page: 5856.

Thesis (Ph.D.)--Yale University, 2005.

This dissertation describes the design and optimization of novel protein-protein interaction (PPI) inhibitors which consist of beta-peptides. beta-peptides are non-natural molecules which fold in a manner similar to natural peptides and proteins. The propensity for beta-peptides to fold into a specific helical conformation, the 14-helix, was analyzed in a systematic way using spectroscopic methods and NMR structural analysis. Insights gained from the biophysical analyses were then applied to the design of inhibitors of the p53•hDM2 interaction, an important target for new cancer therapies. These molecules represent the first beta-peptide helices which bind a cellular protein and inhibit a discrete PPI. Finally, the first high-throughput method for the discovery and optimization of beta-peptide PPI inhibitors was developed, paving the way for broad evaluation of designed beta-peptides as a new and promising class of PPI inhibitors.

ISBN: 9780542394393Subjects--Topical Terms:

1019105
Biophysics, General.

Beta-peptides as inhibitors of protein-protein interactions.
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520 $a This dissertation describes the design and optimization of novel protein-protein interaction (PPI) inhibitors which consist of beta-peptides. beta-peptides are non-natural molecules which fold in a manner similar to natural peptides and proteins. The propensity for beta-peptides to fold into a specific helical conformation, the 14-helix, was analyzed in a systematic way using spectroscopic methods and NMR structural analysis. Insights gained from the biophysical analyses were then applied to the design of inhibitors of the p53•hDM2 interaction, an important target for new cancer therapies. These molecules represent the first beta-peptide helices which bind a cellular protein and inhibit a discrete PPI. Finally, the first high-throughput method for the discovery and optimization of beta-peptide PPI inhibitors was developed, paving the way for broad evaluation of designed beta-peptides as a new and promising class of PPI inhibitors.
520 $a Chapter 1 describes the design and optimization of miniature protein ligands for hDM2. A previously optimized miniature protein, p05, was further evolved using monovalent phage display in order to develop more potent hDM2 ligands. Several functional miniature proteins were gleaned from the selection. Chapter 2 describes a rigorous host-guest analysis of 14-helix folding propensities of various beta3-amino acids. Chapter 3 details the rational design and characterization of 14-helical beta-peptide ligands for hDM2, including the potent molecule beta53-1. Chapter 4 highlights the development and application of a novel one-bead-one-beta-peptide (OBObeta) method for the rapid discovery and optimization of new beta-peptide PPI inhibitors.
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