Εξειδίκευση τύπου :	Περίληψη σε συνέδριο
Τίτλος:	Synthesis of Na-hydrazino- and Aza-peptoids based on substance P: C-terminal fragments and their trypsin inhibitory effect
Δημιουργός/Συγγραφέας:	Ziovas, M. Vakalopoulou, P. Glezakos, P. Papi, R. Stavropoulos, G. [EL] Κυριακίδης, Δ.Α.[EN] Kyriakidis, D.A.
Εκδότης:	Springer
Ημερομηνία:	2009-07
Γλώσσα:	Αγγλικά
ISSN:	0939-4451
DOI:	10.1007/s00726-009-0320-1
Περίληψη:	Serine protease inhibitors (Serpins) is a group of proteins with similar structures, which were first identified as a set of proteins able to inhibit proteases function. The human plasma proteins antithrombin and antitrypsin, which play key roles in controlling blood coagulation and inflammation, respectively, were the first members of the serpins superfamily to be extensively studied. Trypsin-like serine proteases are essential for many biological processes. Because of this a large number of synthetic peptides have been designed and synthesized, based on the structure of inhibitors, active against trypsin or chymotrypsin. In the present work we have synthesized a series of Na-hydrazinopeptoids and aza-peptoids and studied their trypsin inhibitory effect. These peptidomimetics are expected to show enhanced metabolitic stability and bioavailability in comparison with natural parent peptidic analogs. All the syntheses were carried out stepwise by SPPS, using the Fmoc/ But methodology on the solid support 2-chlorotrityl chloride resin and DIC/HOBt as coupling reagent. The products were purified (HPLC) and identified (ESI-MS). Their inhibitory effect against trypsin activity has partly measured, while other compounds are under investigation.
Τίτλος πηγής δημοσίευσης:	Amino Acids 37:(S1):45-45; 11th International Congress on Amino Acids Peptides and Proteins, Vienna, Austria 2009, August 3–7, 2009
Θεματική Κατηγορία:	[EL] Χημεία (Γενικά)[EN] Chemistry (General) [EL] Βιολογία (Γενικά)[EN] Biology (General)
Ηλεκτρονική διεύθυνση περιοδικού (link) :	http://www.springerlink.com/content/104405/
Σημειώσεις:	This work was partly supported by the Research Committee of the University of Patras. Abstract
Εμφανίζεται στις συλλογές:	Άλλα