Total chemical synthesis by native chemical ligation of the all-D immunoglobulin-like domain 2 of Axl |
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Authors: | Lucia De Rosa Rossella Di Stasi Luca Domenico DAndrea |
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Institution: | Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, 80134 Napoli, Italy |
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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. |
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Keywords: | Native chemical ligation Thioester peptide Hydrazide peptide Mirror image |
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