Designed Proteins as Optimized Oxygen Carriers for Artificial Blood
Abstract
This project concerns the transformation of a de novo designed oxygen transport protein into an effective blood substitute. Second year accomplishments include: (A) The creation and verification of a theoretical model for oxyferrous state lifetimes in oxygen transport proteins. (B) We have modified global protein dynamics to double of oxyferrous state lifetime. (C) We have used surface side chain charges to increase the reduction potential of the bound cofactor and triple the oxyferrous state lifetime. (D) We have incorporated an optimized cofactor binding site and shown that the decrease in protein core dynamics increases the lifetime four-fold. (E) We have made significant progress on the determination of the three-dimensional structure of one of the best performing variants. After a limited amount of additional optimization, this protein is ready for incorporation into the crosslinked particles that are the goal of year three.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2013
- Accession Number
- ADA574241
Entities
People
- Ronald L. Koder
Organizations
- City College of New York