Elastin-like polypeptide (ELP) tags for self-assembly and high-throughput processing of functional protein materials

The diverse recognition and catalytic capabilities of globular proteins makes these biomolecules promising candidates in a broad array of applications, including industrial production of commodity chemicals, point-of-care diagnostics, and therapeutics. Self-assembly of globular protein-polymer bioconjugates into nanostructured materials is an attractive protein immobilization strategy that allows for both high protein packing density and control over protein orientation in the material. However, challenges associated with protein-polymer bioconjugate preparation limit the use of these materials in high-throughput processes. This thesis focuses on overcoming this challenge by replacing the polymer block of these bioconjugate materials with a genetically fused elastin-like polypeptide (ELP) tag. The first part of this thesis explores the effects of ELP charge and hydrophobicity on the self-assembly of ELP-mCherry fusion proteins in concentrated solution.

Name thesis:degree_name

Doctoral

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Chemical Engineering

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2019

Author dc:creator

• Mills, Carolyn Elaine.

Advisor dc:contributor.advisor

• Bradley D. Olsen.

• Chemical Engineering.

Statement dc:rights

• MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

https://hdl.handle.net/1721.1/123726

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/123726