Skip navigation
Please use this identifier to cite or link to this item: http://arks.princeton.edu/ark:/88435/dsp01bz60cz71d
Title: Construction of Fusion Lasso Peptides with Pharmaceutically-Relevant Sequences
Authors: Hubbell, Kenneth Tyler
Advisors: Link, A. James
Department: Chemical and Biological Engineering
Class Year: 2016
Abstract: The promise of small, potent peptide drugs is currently limited by the vulnerability of peptides to proteolysis in the human body. This work demonstrates the potential of highly stable lasso peptides to serve as “scaffolds” for pharmaceutically-relevant sequences. The unique structure of lasso peptides grants them natural resistance to thermal, chemical, and enzymatic degradation, but the maturation enzymes which form this structure are highly sensitive to alterations in the lasso precursor sequence. Previous work had found that the lasso astexin-1 may form even when fused to the leucine zipper A1. Present work expanded on that system to introduce the pharmaceutically-attractive VEGF-binding sequence IHVMWEWECFERL into a disulfide-constrained loop in the tail of astexin-1. The resulting fusion peptide was found to bind VEGF.
Extent: 53 pages
URI: http://arks.princeton.edu/ark:/88435/dsp01bz60cz71d
Type of Material: Princeton University Senior Theses
Language: en_US
Appears in Collections:Chemical and Biological Engineering, 1931-2016

Files in This Item:
File SizeFormat 
HUBBELL_Kenneth_CBE_Senior_Thesis_2016.pdf1.66 MBAdobe PDF    Request a copy


Items in Dataspace are protected by copyright, with all rights reserved, unless otherwise indicated.