DEVELOPMENT OF A SITE-SPECIFIC GLYCOLIGATION TO SYNTHESIZE RECOMBINANT N-GLYCOPROTEINS VIA THIOACID CAPTURE LIGATION

Daniel Collins

Back

DEVELOPMENT OF A SITE-SPECIFIC GLYCOLIGATION TO SYNTHESIZE RECOMBINANT N-GLYCOPROTEINS VIA THIOACID CAPTURE LIGATION

Dissertation

Open access

DEVELOPMENT OF A SITE-SPECIFIC GLYCOLIGATION TO SYNTHESIZE RECOMBINANT N-GLYCOPROTEINS VIA THIOACID CAPTURE LIGATION

Daniel Collins

Doctor of Philosophy (PhD), Washington State University

01/2020

Handle:

https://hdl.handle.net/2376/118354

Files and links (1)

pdf

collins-dissertation[1]9.15 MBDownload View

Open Access

Abstract

glycoligation

glycoprotein

N-glycoprotein

native chemical ligation

recombinant protein

thioacid capture ligation

The goal of the project was to synthesize asparagine-linked glycoproteins with a natural linkage. We described an aspartyl thioester unnatural amino acid and its incorporation into a recombinant protein. Its utility was demonstrated by native chemical ligation. Attempts to transform the aspartyl thioester into an asparagine-linked glycoprotein with a natural linkage were unsuccessful. Hydrolysis was observed.

Metrics

16 File views/ downloads

23 Record Views

Details

Title: DEVELOPMENT OF A SITE-SPECIFIC GLYCOLIGATION TO SYNTHESIZE RECOMBINANT N-GLYCOPROTEINS VIA THIOACID CAPTURE LIGATION
Creators: Daniel Collins
Contributors: Philip P Garner (Advisor)
Gregory J Crouch (Committee Member)
Rock J Mancini (Committee Member)
Ming Xian (Committee Member)
Awarding Institution: Washington State University
Academic Unit: Chemistry, Department of
Theses and Dissertations: Doctor of Philosophy (PhD), Washington State University
Number of pages: 204
Identifiers: 99900581412501842
Language: English
Resource Type: Dissertation