171778-09-9

Basic information

• Product Name: FMOC-ASP(OBUT)-NH2
• Synonyms: N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-L-ISOASPARAGINE T-BUTYL ESTER;N-ALPHA-(9-FLUORENYLMETHYLOXYCARBONYL)-L-ASPARTAMIDE BETA-TERT-BUTYL ESTER;FMOC-L-ISOASN-OTBU;FMOC-L-ISOASPARAGINE BETA-T-BUTYL ESTER;FMOC-L-ASP(TBU)-NH2;FMOC-ISOASN(BUT)-OH;FMOC-ISOASN(TBU)-OH;FMOC-ISOASPARAGINE T-BUTYL ESTER
• CAS NO: 171778-09-9
• Molecular Formula: C₂₃H₂₆N₂O₅
• Molecular Weight: 410.46
• Mol File: 171778-09-9.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: FMOC-ASP(OBUT)-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-ASP(OBUT)-NH2(171778-09-9)
• EPA Substance Registry System: FMOC-ASP(OBUT)-NH2(171778-09-9)

Safety Data

• Hazardous Substances Data: 171778-09-9(Hazardous Substances Data)

Upstream product

• 71989-14-5 Fmoc-(tBu)Asp-OH 

Downstream Products

• 1051922-97-4 C₃₁H₃₆N₂O₇ 

Relevant articles and documents

Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein

Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.