Bound Volume Number
Volume II
Degree Type
Honors Capstone Project
Date of Submission
Spring 5-2016
Capstone Advisor
Ivan Korendovych
Capstone Major
Biomedical and Chemical Engineering
Capstone College
Arts and Science
Audio/Visual Component
no
Keywords
Proteins, de novo, three- dimensional structures
Capstone Prize Winner
no
Won Capstone Funding
yes
Honors Categories
Sciences and Engineering
Subject Categories
Biochemistry
Abstract
Proteins carry out many extremely efficient functions, including catalysis and biomolecule recognition. Underlying this efficiency is their extraordinary complexity and ability to fold into unique three-dimensional structures. Attempts to replicate this efficiency through de novo design have only shown moderate success, and it is unclear how modern-day proteins may have evolved. However, short peptides that alternate hydrophobic and hydrophilic residues can self-assemble into amyloid fibrils to achieve well-defined secondary structure. These aggregates may have served as a template from which the first proteins were derived. We designed self-assembling seven-residue peptides that are able to act as Zn2+-dependent esterases. Zn2+ acts to both help induce fibril formation and to serve as a metal cofactor to catalyze acyl ester hydrolysis. Furthermore, we developed a second set of peptides to recognize a target molecule with moderate specificity. The ability of this simple system to catalyze a chemical reaction and exhibit biomolecule recognition suggests that similar peptide aggregates may have been evolutionary precursors to modern-day proteins. Additionally, the ability to use a minimalistic design approach to generate functional fibrils could have implications for the development of simple nanostructured biomaterials. By using an alternating hydrophobic/hydrophilic template, novel functionality can be introduced into simple peptide aggregates.
Recommended Citation
Smith, Tyler, "Using Simple Self-Assembling Peptides to Attain Novel Protein-Like Functions" (2016). Renée Crown University Honors Thesis Projects - All. 931.
https://surface.syr.edu/honors_capstone/931
Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.
