Stepwise triple-click functionalization of synthetic peptides

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00493563" target="_blank" >RIV/61388963:_____/18:00493563 - isvavai.cz</a>

Výsledek na webu

<a href="http://pubs.rsc.org/en/content/articlehtml/2018/ob/c8ob01617h" target="_blank" >http://pubs.rsc.org/en/content/articlehtml/2018/ob/c8ob01617h</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c8ob01617h" target="_blank" >10.1039/c8ob01617h</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Stepwise triple-click functionalization of synthetic peptides

Popis výsledku v původním jazyce

The increasing popularity of peptides as promising molecular scaffolds for biomedical applications and as valuable biochemical probes makes new methods allowing for their modification highly desirable. We describe herein an optimized protocol based on a sequence of CuAAC click reactions and selective deprotection steps, which leads to an efficient multi-functionalization of synthetic peptides. The methodology has been successfully applied to the construction of defined heteroglycopeptides and fluorophore-quencher-containing probes for proteases. The developed chemistry thus represents an important addition to the available toolbox of methods enabling efficient postsynthetic modification of peptides. The commercial availability of numerous azide probes further greatly extends the application potential of the described methodology.

Název v anglickém jazyce

Stepwise triple-click functionalization of synthetic peptides

Popis výsledku anglicky

The increasing popularity of peptides as promising molecular scaffolds for biomedical applications and as valuable biochemical probes makes new methods allowing for their modification highly desirable. We describe herein an optimized protocol based on a sequence of CuAAC click reactions and selective deprotection steps, which leads to an efficient multi-functionalization of synthetic peptides. The methodology has been successfully applied to the construction of defined heteroglycopeptides and fluorophore-quencher-containing probes for proteases. The developed chemistry thus represents an important addition to the available toolbox of methods enabling efficient postsynthetic modification of peptides. The commercial availability of numerous azide probes further greatly extends the application potential of the described methodology.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10401 - Organic chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Organic & Biomolecular Chemistry

ISSN

1477-0520

e-ISSN

—

Svazek periodika

16

Číslo periodika v rámci svazku

33

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

5

Strana od-do

5960-5964

Kód UT WoS článku

000442510500003

EID výsledku v databázi Scopus

2-s2.0-85052389429