Axl is a tyrosine kinases receptor playing crucial role in several cellular responses. The deregulation of Axl signaling has been associated to many high impact diseases ranging from cancer to multiple sclerosis. We report the successful procedure for the chemical synthesis of the Ig2 domain of Axl, one of the key extracellular regions of the receptor involved in ligand binding. The protein was synthesized in its D-enantiomeric form (D-Axl-2), opening the way to the selection of D-peptides selectively targeting Axl receptor through the mirror-image phage display peptide library screening approach. (C) 2019 Elsevier Ltd. All rights reserved.

Total chemical synthesis by native chemical ligation of the all-D immunoglobulin-like domain 2 of Axl

De Rosa Lucia
Primo
;
Di Stasi Rossella;D'Andrea Luca Domenico
2019

Abstract

Axl is a tyrosine kinases receptor playing crucial role in several cellular responses. The deregulation of Axl signaling has been associated to many high impact diseases ranging from cancer to multiple sclerosis. We report the successful procedure for the chemical synthesis of the Ig2 domain of Axl, one of the key extracellular regions of the receptor involved in ligand binding. The protein was synthesized in its D-enantiomeric form (D-Axl-2), opening the way to the selection of D-peptides selectively targeting Axl receptor through the mirror-image phage display peptide library screening approach. (C) 2019 Elsevier Ltd. All rights reserved.
2019
Istituto di Biostrutture e Bioimmagini - IBB - Sede Napoli
Thioester peptide, Thioester peptide, Hydrazide peptide, Mirror image
Hydrazide peptide
Mirror image
Native chemical ligation
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/383006
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