96920-81-9

Basic information

• Product Name: 2,5-Pyrrolidinedione, 1-[[2,3-bis(phenylmethoxy)benzoyl]oxy]-
• CAS NO: 96920-81-9
• Molecular Formula: C25H21NO6
• Molecular Weight: 431.445
• Mol File: 96920-81-9.mol
• Article Data: 7

Chemical Properties

• CAS DataBase Reference: 2,5-Pyrrolidinedione, 1-[[2,3-bis(phenylmethoxy)benzoyl]oxy]-(CAS DataBase Reference)
• NIST Chemistry Reference: 2,5-Pyrrolidinedione, 1-[[2,3-bis(phenylmethoxy)benzoyl]oxy]-(96920-81-9)
• EPA Substance Registry System: 2,5-Pyrrolidinedione, 1-[[2,3-bis(phenylmethoxy)benzoyl]oxy]-(96920-81-9)

Safety Data

• Hazardous Substances Data: 96920-81-9(Hazardous Substances Data)

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 74272-78-9 2,3-dibenzyloxybenzoic acid 
• 303-38-8 2,3-Dihydroxybenzoic acid 
• 100-39-0 benzyl bromide 
• 24677-78-9 2,3-dihydroxybenzaldehyde 
• 100-44-7 benzyl chloride 

Downstream Products

• 123198-04-9 N-<2,3-bis(benzyloxy)benzoyl>-L-alanine 
• 74272-79-0 N-(2,3-dibenzyloxybenzoyl)-L-threonine 
• 123198-13-0 2,3-dibenzyloxybenzoyl-Ala-Orn(Ac)-OBzl 
• 123198-14-1 2,3-dibenzyooxybenzoyl-Ala-Orn(Z)-OBzl 
• 123198-06-1 2,3-dibenzyloxybenzoyl-Ala-Thr-OBzl 
• 88167-28-6 2,3-dihydroxybenzoyl-L-alanyl-L-threonine 
• 123198-09-4 2,3-dibenzyloxybenzoyl-Ala-Leu-OH 
• 123198-15-2 2,3-dibenzyloxybenzoyl-Thr-Ala-OH 
• 123198-11-8 2,3-dibenzyloxybenzoyl-Ala-Phe-OH 
• 939794-65-7 C₃₄H₃₄N₆O₉S 
• 1304495-13-3 N,N'-[(R)-5-[[2-[[(S)-1-(benzyloxy)-2-oxopiperidin-3-yl]amino]-2-oxoethyl]amino]-5-oxopentane-1,4-diyl]bis[2,3-bis(benzyloxy)benzamide] 
• 1202365-63-6 Nocardia heterobactin 
• 238081-25-9 (R)-2,5-bis[2,3-bis(benzyloxy)benzamido]pentanoic acid 
• 1304495-10-0 tert-butyl [(R)-1-[[2-[[(S)-1-(benzyloxy)-2-oxopiperidin-3-yl]amino]-2-oxoethyl]amino]-5-[2,3-bis(benzyloxy)benzamido]-1-oxopentan-2-yl]carbamate 

Relevant articles and documents

Defining the Catechol-Cation Synergy for Enhanced Wet Adhesion to Mineral Surfaces

Mussel foot proteins (Mfps) exhibit remarkably adaptive adhesion and bridging between polar surfaces in aqueous solution despite the strong hydration barriers at the solid-liquid interface. Recently, catechols and amines - two functionalities that account

Impact of Molecular Architecture and Adsorption Density on Adhesion of Mussel-Inspired Surface Primers with Catechol-Cation Synergy

Marine mussels secrete proteins rich in residues containing catechols and cationic amines that displace hydration layers and adhere to charged surfaces under water via a cooperative binding effect known as catechol-cation synergy. Mussel-inspired adhesives containing paired catechol and cationic functionalities are a promising class of materials for biomedical applications, but few studies address the molecular adhesion mechanism(s) of these materials. To determine whether intramolecular adjacency of these functionalities is necessary for robust adhesion, a suite of siderophore analog surface primers was synthesized with systematic variations in intramolecular spacing between catechol and cationic functionalities. Adhesion measurements conducted with a surface forces apparatus (SFA) allow adhesive failure to be distinguished from cohesive failure and show that the failure mode depends critically on the siderophore analog adsorption density. The adhesion of these molecules to muscovite mica in an aqueous electrolyte solution demonstrates that direct intramolecular adjacency of catechol and cationic functionalities is not necessary for synergistic binding. However, we show that increasing the catechol-cation spacing by incorporating nonbinding domains results in decreased adhesion, which we attribute to a decrease in the density of catechol functionalities. A mechanism for catechol-cation synergy is proposed based on electrostatically driven adsorption and subsequent binding of catechol functionalities. This work should guide the design of new adhesives for binding to charged surfaces in saline environments.

Synthesis of heterobactins A and B and Nocardia heterobactin

The synthesis of the Rhodococcus erythropolis siderophores heterobactins A and B, and the structurally related Nocardia heterobactin, is described. Two approaches for the assembly of these asymmetric ligand donor chelators are explored. In the first approach, a scheme predicated on the biosynthesis of the Paracoccus denitrificans siderophore, parabactin, is employed. In this approach, the central donor synthon is added last. In the second scheme, the central donor and the terminal 2,3-dihydroxybenzoyl fragment are first fixed to the ligand's d-ornithine backbone. This is followed by condensation with the cyclic ornithine hydroxamate glycine segment. The schemes offer a flexible approach to other heterobactins. Job's plots suggest that heterobactin A and Nocardia heterobactin form 1:1 ligand/metal complexes, while heterobactin B forms a 3:2 ligand/metal complex.