96920-81-9

Upstream product

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

Downstream Products

• 123198-04-9 N-<2,3-bis(benzyloxy)benzoyl>-L-alanine 
• 939794-65-7 C₃₄H₃₄N₆O₉S 
• 74272-79-0 N-(2,3-dibenzyloxybenzoyl)-L-threonine 
• 1304495-09-7 (R)-5-[2,3-bis(benzyloxy)benzamido]-2-[(tert-butoxycarbonyl)amino]pentanoic acid 
• 1202365-63-6 Nocardia heterobactin 
• 363624-56-0 heterobactin A 
• 363624-57-1 heterobactin B 
• 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] 
• 1304495-12-2 N-[(R)-1-[[2-[[(S)-1-(benzyloxy)-2-oxopiperidin-3-yl]amino]-2-oxoethyl]amino]-5-[2,3-bis(benzyloxy)benzamido]-1-oxopentan-2-yl]-5-hydroxy-4-benzoxazolecarboxamide 
• 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 
• 238081-25-9 (R)-2,5-bis[2,3-bis(benzyloxy)benzamido]pentanoic acid 
• 123198-13-0 2,3-dibenzyloxybenzoyl-Ala-Orn(Ac)-OBzl 
• 123198-06-1 2,3-dibenzyloxybenzoyl-Ala-Thr-OBzl 
• 123198-11-8 2,3-dibenzyloxybenzoyl-Ala-Phe-OH 

Relevant academic research and scientific papers

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

Nanomechanics of Anion-πInteraction in Aqueous Solution

Noncovalent interactions play a constitutive role in numerous biological processes, including biomolecular adhesion, recognition, and transport. Unlike π-πand cation-πinteractions, anion-πinteraction was only recently and computationally recognized to par

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.

Mimicking salmochelin S1 and the interactions of its Fe(III) complex with periplasmic iron siderophore binding proteins CeuE and VctP

A mimic of the tetradentate stealth siderophore salmochelin S1, was synthesised, characterised and shown to form Fe(III) complexes with ligand-to-metal ratios of 1:1 and 3:2. Circular dichroism spectroscopy confirmed that the periplasmic binding proteins

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.

Antibacterial Agents

The invention provides compounds of formula (I) and salts thereof: R1-L-R2—B wherein R1, L, R2, and B have any of the values defined herein, as well as compositions comprising such compounds, and therapeutic methods comprising the administration of such compounds or salts. The compounds block siderophore production in bacteria and are useful as antibacterial agents.

5′-O-[(N-acyl)sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: An adenylation enzyme required for siderophore biosynthesis of the mycobactins

A study of the structure - activity relationships of 5′-O-[N- (salicyl)sulfamoyl]adenosine (6), a potent inhibitor of the bifunctional enzyme salicyl-AMP ligase (MbtA, encoded by the gene Rv2384) in Mycobacterium tuberculosis, is described, targeting the salicyl moiety. A systematic series of analogues was prepared exploring the importance of substitution at the C-2 position revealing that a hydroxy group is required for optimal activity. Examination of a series of substituted salicyl derivatives indicated that substitution at C-4 was tolerated. Consequently, a series of analogues at this position provided 4-fluoro derivative, which displayed an impressive MIC 99 of 0.098 μM against whole-cell M. tuberculosis under iron-limiting conditions. Examination of other heterocyclic, cycloalkyl, alkyl, and aminoacyl replacements of the salicyl moiety demonstrated that these nonconserative modifications were poorly tolerated, a result consistent with the fairly strict substrate specificities of related non-ribosomal peptide synthetase adenylation enzymes.