Issue 43, 2010
From the journal:

Chemical Communications

Total chemical synthesis of human proinsulin†‡

Samuel Luisier,§a   Michal Avital-Shmilovici,§a   Michael A. Weissb  and  Stephen B. H. Kent*a  

* Corresponding authors

a Department of Chemistry, Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA
E-mail: skent@uchicago.edu

b Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA
E-mail: michael.weiss@case.edu

Abstract

A convergent synthetic strategy based on modern chemical ligation methods was used to make human proinsulin. The synthetic protein was characterized by LCMS, CD spectroscopy, and by 1D- and 2D-NMR spectroscopy. Synthetic human proinsulin had full biochemical activity in a receptor-binding assay.

Graphical abstract: Total chemical synthesis of human proinsulin

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C0CC03141K
Article type
Communication
Submitted
10 Aug. 2010
Accepted
07 Sept. 2010
First published
28 Sept. 2010

Chem. Commun., 2010,46, 8177-8179

Permissions

Request permissions

Total chemical synthesis of human proinsulin

S. Luisier, M. Avital-Shmilovici, M. A. Weiss and S. B. H. Kent, Chem. Commun., 2010, 46, 8177 DOI: 10.1039/C0CC03141K

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements