249538-93-0

Basic information

• Product Name: N-(benzyloxycarbonylmethyl)-N'-[(2'S)-2'-(methoxycarbonyl)phenethyl]sulfamide
• Synonyms: N-(benzyloxycarbonylmethyl)-N'-[(2'S)-2'-(methoxycarbonyl)phenethyl]sulfamide
• CAS NO: 249538-93-0
• Molecular Weight: 406.459
• Mol File: 249538-93-0.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: N-(benzyloxycarbonylmethyl)-N'-[(2'S)-2'-(methoxycarbonyl)phenethyl]sulfamide(CAS DataBase Reference)
• NIST Chemistry Reference: N-(benzyloxycarbonylmethyl)-N'-[(2'S)-2'-(methoxycarbonyl)phenethyl]sulfamide(249538-93-0)
• EPA Substance Registry System: N-(benzyloxycarbonylmethyl)-N'-[(2'S)-2'-(methoxycarbonyl)phenethyl]sulfamide(249538-93-0)

Safety Data

• Hazardous Substances Data: 249538-93-0(Hazardous Substances Data)

Upstream product

• 139059-69-1 <(S)(+)> methyl -phenylalaninate 
• 1027948-81-7 C₂₄H₃₀N₂O₈S 

Downstream Products

• 249539-20-6 (4S)-5-acetyl-4-benzyl-2-(benzyloxycarbonyl)-1-methyl-3-oxo-1,2,5-thiadiazolidine 1,1-dioxide 
• 249539-09-1 (4S)-4-benzyl-2-(benzyloxycarbonyl)methyl-3-oxo-1,2,5-thiadiazolidine 1,1-dioxide 

Relevant articles and documents

Sulfahydantoins as tripeptide constraints: Synthesis and structure of chiral substituted 3-oxo-1,2,5-thiadiazolidine 1,1-dioxides

A sulfahydantoin (3-oxo-1,2,5-thiadiazohdine 1,1-dioxides) motif is used as a new type of peptidic constraint to lock two consecutive amide nitrogens by a sulfonyl bridge. The 5membered heterocyclic motif was prepared starting from proteogenic and synthetic amino acids and chlorosulfonyl isocyanate. Constrained dipeptides were obtained under alkaline conditions (methoxide or tert-butoxide) by cyclization of symmetric and dissymmetric sulfamides. The absolute configuration of the chiral centers for the derivative L-Phe-D-Ala, a congener of the series, was established by X-ray diffraction crystallographic analysis. In addition, the chemo-, regio-, and stereoselectivities of the reactions were studied. In the acylated derivatives, the sulfahydantoin constraint induces a unique backbone conformation with coplanarity of two consecutive peptide bonds.