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Current Topics in Peptide & Protein Research   Volumes    Volume 1  Issue 1
Site directed disulfide bond formation during the total synthesis of insulin-like molecules
Erika E. Büllesbach
Pages: 75 - 87
Number of pages: 13
Current Topics in Peptide & Protein Research
Volume 1  Issue 1

Copyright © 1994 Research Trends. All rights reserved

Three-dimensional chemical syntheses of proteins have been developed for the total synthesis of insulin-like molecules (insulin, relaxin, and bombyxin). The method used peptide synthesis in combination with a site-directed formation of one intrachain and two interchain disulfide bonds. Although the disulfide synthesis occurs under denaturation conditions the proteins were fully biological active. In order to investigate the structure-function relationship of these hormones a variety of defined analogs were synthesized including insulin derivatives which were not obtainable by the commonly used chain-combination method. This implies that site-directed disulfide formation could be a method of choice to produce small disulfide rich proteins.
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