Advancements in polymer resins for solid-phase peptide synthesis
Name
959716041-MIT.pdf
Description
Full printable version
Size
4.71 MB
Format
Adobe PDF
Checksum (MD5)
0005a70b12400fbb8593cb149ec88891
Author(s)
Hewage, Gihan B. (Gihan Bhagye)
Advisor(s)
Jeremiah A. Johnson.
Date Issued
2016
Publisher
Massachusetts Institute of Technology
Abstract
The use of polymeric supports in solid-phase peptide synthesis has allowed for the facile, rapid synthesis of short peptides in a one bead/one sequence manner. This approach allows for screening peptide libraries for binding and catalytic activities. Once hits are found, the sequence of the active protein can be determined via mass spectrometry. However, problems arise when trying to create large libraries (on the order of 10⁹) of peptides. The resins large enough to provide sufficient amounts of peptide sample for sequencing would occupy too great a volume in order to create large quantities. Conversely, attempting to fold a protein on resins with very high loading results in folding errors. In order to overcome these issues, we attempted to develop a novel core-shell polymer support, containing unprotected amine functional groups at low concentration on the resin surface and a large quantity of an amine, protected orthogonally to the conditions of solid-state peptide synthesis, in the core. In principle, this would allow for the synthesis of a sufficient quantity of fully folded proteins on the resin surface to screen for peptide activity while simultaneously synthesizing enough of the variable sequence in the interior of the resin to allow for a high yield of material for sequence determination.
Description
Thesis: S.M., Massachusetts Institute of Technology, Department of Chemistry, 2016.
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 28-30).
Subjects
Chemistry.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
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