Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475234" target="_blank" >RIV/61388963:_____/17:00475234 - isvavai.cz</a>

Result on the web

<a href="http://onlinelibrary.wiley.com/doi/10.1002/psc.2968/full" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/psc.2968/full</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/psc.2968" target="_blank" >10.1002/psc.2968</a>

Result language

angličtina

Original language name

Optimized syntheses of Fmoc azido amino acids for the preparation of azidopeptides

Original language description

The rise of CuI-catalyzed click chemistry has initiated an increased demand for azido and alkyne derivatives of amino acid as precursors for the synthesis of clicked peptides. However, the use of azido and alkyne amino acids in peptide chemistry is complicated by their high cost. For this reason, we investigated the possibility of the in-house preparation of a set of five Fmoc azido amino acids: beta-azido L-alanine and D-alanine,gamma-azido L-homoalanine, delta-azido L-ornithine and omega-azido L-lysine. We investigated several reaction pathways described in the literature, suggested several improvements and proposed several alternative routes for the synthesis of these compounds in high purity. Here, we demonstrate that multigram quantities of these Fmoc azido amino acids can be prepared within a week or two and at user-friendly costs. We also incorporated these azido amino acids into several model tripeptides, and we observed the formation of a new elimination product of the azido moiety upon conditions of prolonged couplings with 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate/DIPEA. We hope that our detailed synthetic protocols will inspire some peptide chemists to prepare these Fmoc azido acids in their laboratories and will assist them in avoiding the too extensive costs of azidopeptide syntheses. Experimental procedures and/or analytical data for compounds 3-5, 20, 25, 26, 30 and 43-47 are provided in the supporting information.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

<a href="/en/project/GA14-17305S" target="_blank" >GA14-17305S: Insulin mimetics</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Peptide Science

ISSN

1075-2617

e-ISSN

—

Volume of the periodical

23

Issue of the periodical within the volume

3

Country of publishing house

GB - UNITED KINGDOM

Number of pages

13

Pages from-to

202-214

UT code for WoS article

000397279800001

EID of the result in the Scopus database

2-s2.0-85015131428