482631-85-6

Basic information

• Product Name: (2S)-1-benzyl 4-tert-butyl 2-(((9H-fluoren-9-yl)(phenyl)methyl)amino)succinate
• Synonyms: (2S)-1-benzyl 4-tert-butyl 2-(((9H-fluoren-9-yl)(phenyl)methyl)amino)succinate
• CAS NO: 482631-85-6
• Molecular Weight: 519.64
• Mol File: 482631-85-6.mol

Chemical Properties

• CAS DataBase Reference: (2S)-1-benzyl 4-tert-butyl 2-(((9H-fluoren-9-yl)(phenyl)methyl)amino)succinate(CAS DataBase Reference)
• NIST Chemistry Reference: (2S)-1-benzyl 4-tert-butyl 2-(((9H-fluoren-9-yl)(phenyl)methyl)amino)succinate(482631-85-6)
• EPA Substance Registry System: (2S)-1-benzyl 4-tert-butyl 2-(((9H-fluoren-9-yl)(phenyl)methyl)amino)succinate(482631-85-6)

Safety Data

• Hazardous Substances Data: 482631-85-6(Hazardous Substances Data)

Upstream product

• 100-39-0 benzyl bromide 
• 482632-06-4 2-(9-phenyl-9H-fluoren-9-ylamino)-succinic acid 4-tert-butyl ester 
• 55135-66-5 9-bromo-9-phenyl-9H-fluorene 
• 3057-74-7 L-Asp(t-Bu) 

Relevant articles and documents

Total Synthesis of Skyllamycins A–C

The skyllamycins are a family of highly functionalized non-ribosomal cyclic depsipeptide natural products which contain the extremely rare α-OH-glycine functionality. Herein the first total synthesis of skyllamycins A–C is reported, together with the biofilm inhibitory activity of the natural products. Linear peptide precursors for each natural product were prepared through an efficient solid-phase route incorporating a number of synthetic modified amino acids. A novel macrocyclization step between a C-terminal amide and an N-terminal glyoxylamide moiety served as a key transformation to install the unique α-OH-glycine unit and generate the natural products in the final step of the synthesis.

Incorporation of (2S,3S) and (2S,3R) β-methyl aspartic acid into RGD-containing peptides

We report the synthesis and biological activity of a series of side-chain-constrained RGD peptides containing the (2S,3R) or (2S,3S) β-methyl aspartic acid within the RGD sequence. These compounds have been assayed for binding to the integrin receptors αIIbβ3 and αvβ3 and the results demonstrate the importance of the side-chain orientation of this particular residue within the RGD sequence. Based on our findings, the (2S,3S) β-methylated analogues of our RGD sequences maintain their binding potency to the integrin receptors while the (2S,3R) β-methylated analogues exhibit a drastically reduced binding affinity. Our studies demonstrate that the three-dimensional orientation of the aspartyl side chain is a very important parameter for integrin binding and that small changes that affect the side-chain orientations give rise to drastic changes in binding affinity. These results provide important information for the design of more potent RGD mimetics. Copyright