1946-80-1

Upstream product

• 98-88-4 benzoyl chloride 
• 1155-64-2 N₆-[(benzyloxy)carbonyl]-L-lysine 
• 65-85-0 benzoic acid 
• 23405-15-4 benzoic acid N-hydroxysuccinimide ester 

Downstream Products

• 366-74-5 N^α-benzoyl-L-lysine 
• 33869-64-6 α-N-Benzoyl-ε-N-carbobenzoxy-L-lysin-tert-butylester 
• 94859-79-7 methyl 3-α-benzoyl-N^ε-(benzyloxycarbonyl)lysinyl>propionate 
• 106746-02-5 Phenylmethyl N-<5-(Benzoylamino)-5-(trifluoroacetyl)pentyl>carbamate 
• 106942-42-1 {4-[5-Oxo-2-phenyl-4-(2,2,2-trifluoro-acetyl)-4,5-dihydro-oxazol-4-yl]-butyl}-carbamic acid benzyl ester 
• 123003-97-4 Phenylmethyl N-<4-(4,5-dihydro-5-oxo-2-phenyl-4-oxazoyl)butyl>carbamate 
• 33869-65-7 6-Amino-2-benzyloxycarbonylaminohexanoic acid tert-butyl ester 

Relevant academic research and scientific papers

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.

KETONE INHIBITORS OF LYSINE GINGIPAIN

The present invention provides compounds according to Formula (I) as described herein, and their use for inhibiting the lysine gingipain protease (Kgp) from the bacterium Porphyromonas gingivalis. Also described are gingipain activity probe compounds and methods for assaying gingipain activity are also described, as well as methods for the treatment of disorders associated with P. gingivalis infection, including brain disorders such as Alzheimer's disease.

DIISOPROPYLETHYLAMINE ELIMINATES DIPEPTIDE FORMATION DURING THE ACYLATION OF AMINO ACIDS USING BENZOYL CHLORIDE AND SOME ALKYL CHLOROFORMATES

Acylation of amino acids using benzoyl chloride in aqueous alkali leads to benzoylamino acids containing one percent of benzoyldipeptide.Use of diisopropylethylamine instead of sodium hydroxide as base eliminates the side reaction responsible for the contaminant.Ethoxycarbonylamino acids are advantageously prepared in the same manner using ethyl chloroformate or diethyl dicarbonate.The latter gives rise to some N-substituted dipeptide when used in aqueous alkali.The method is unsatisfactory for the benzyloxycarbonylation of amino acids.Use of 9-fluorenylmethyl chloroformate and diisopropylethylamine gives the pure derivative of leucine in moderate yield.

SUBSTITUTED PEPTIDE COMPOUNDS

Substituted peptide compounds of the formula STR1 are disclosed. These compounds are useful as hypotensive agents due to their angiotensin converting enzyme inhibition activity and depending upon the definition of X may also be useful as analgesics due to their enkephalinase inhibition activity.