Synthesis, analysis and biological evaluation of new RGD mimetics

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00485824" target="_blank" >RIV/61388963:_____/17:00485824 - isvavai.cz</a>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Synthesis, analysis and biological evaluation of new RGD mimetics

Popis výsledku v původním jazyce

The amino acid sequence L-arginyl-glycyl-L-aspartic acid (RGD) is a part of many extracellular proteins. It is a specific recognition site by integrins. Some synthetic RGD analogues bind specifically with integrin receptors on the cell membrane, which are over-expressed on the surface of various malignant human tumour and angiogenic endothelial cells. These peptides exert dual role by: inhibiting proliferation and migration of tumour cells and on the other hand by inhibiting angiogenesis. In recent years, many RGD cytotoxic agents have been developed, that showed promising results in vitro and in vivo. Herein we present the synthesis, analysis and biological evaluation of two new RGD analogues, modified in position 1 with Arg mimetics (Agb or Agp). Our pilot studies on their cytotoxicity were presented in comparison to parent RGD as standard.

Název v anglickém jazyce

Synthesis, analysis and biological evaluation of new RGD mimetics

Popis výsledku anglicky

The amino acid sequence L-arginyl-glycyl-L-aspartic acid (RGD) is a part of many extracellular proteins. It is a specific recognition site by integrins. Some synthetic RGD analogues bind specifically with integrin receptors on the cell membrane, which are over-expressed on the surface of various malignant human tumour and angiogenic endothelial cells. These peptides exert dual role by: inhibiting proliferation and migration of tumour cells and on the other hand by inhibiting angiogenesis. In recent years, many RGD cytotoxic agents have been developed, that showed promising results in vitro and in vivo. Herein we present the synthesis, analysis and biological evaluation of two new RGD analogues, modified in position 1 with Arg mimetics (Agb or Agp). Our pilot studies on their cytotoxicity were presented in comparison to parent RGD as standard.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Bulgarian Chemical Communications

ISSN

0324-1130

e-ISSN

—

Svazek periodika

49

Číslo periodika v rámci svazku

SI E

Stát vydavatele periodika

BG - Bulharská republika

Počet stran výsledku

4

Strana od-do

7-10

Kód UT WoS článku

000418303600002

EID výsledku v databázi Scopus

—