Activation of cathepsin D by glycine ethyl ester

Glycine ethyl ester hydro­chloride

In the crystal structure of the title compound, C(4)H(10)NO(2) (+)·Cl(-) (systematic name: 3-eth-oxy-3-oxopropan-1-aminium chlor-ide), there are strong inter-molecular N-H⋯Cl, C-H⋯Cl and C-H⋯O hydrogen-bonding inter-actions between the free chloride anion and the organic cation, resulting in a two-dimensional supra-molecular network in the ab plane.

The Apparent Dissociation Constant of Glycine Ethyl Ester.*

According to the classical theory of the dissociation of weak electrolytes, the amino acids show much lower basic and acidic dissociation constants than would be expected from a comparison with other weak acids and bases. In order to explain this anomaly, Adams (1) originally suggested that an ampholyte must necessarily exist almost entirely as an “inner salt.” Bjerrum (2) extended this idea wi...

Regulation of Cathepsin D Activity and Activation

Glycine methyl ester hydro­chloride

THE TITLE COMPOUND [SYSTEMATIC NAME: (methoxy-carbonyl-meth-yl)ammonium chloride], crystallizes as a salt, C(3)H(8)NO(2) (+)·Cl(-), with the charged species inter-acting mutually via strong and highly directional N(+)-H⋯Cl(-) hydrogen bonds which lead to the formation of a supra-molecular tape running parallel to the c axis. Tapes close pack in the solid state mediated by multipoint recognition...

Inhibition of cathepsin D by synthetic oligopeptides.

A number of synthetic oligopeptides with the COOH terminus D-amino acid situated third from the potentially cleavable phenylalanyl-phenylalanyl bond, typified by < Glu-D-Phe-Pro-Phe-Phe-Val-D-Trp (Peptide VI) were shown to be potent competitive inhibitors of cathepsin D and pepsin. Peptide VI, which forms an equimolar nonproductive enzyme l inhibitor complex, inhibited the hydrolysis of methyl[...