BIOMAT Database Logo BIOMAT Database Logo

Modified peptides which display potent and specific inhibition of human renin. 1987

J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun

A new class of angiotensinogen analogues which contain heteroatom-methylene and retro-inverso amide bond replacements was synthesized and evaluated for renin inhibition. Selected compounds in the series were specific for renin over other aspartic proteinases, and the most potent inhibitor demonstrated hypotensive activity in a salt depleted monkey.

UI MeSH Term Description Entries
D007202 Indicators and Reagents Substances used for the detection, identification, analysis, etc. of chemical, biological, or pathologic processes or conditions. Indicators are substances that change in physical appearance, e.g., color, at or approaching the endpoint of a chemical titration, e.g., on the passage between acidity and alkalinity. Reagents are substances used for the detection or determination of another substance by chemical or microscopical means, especially analysis. Types of reagents are precipitants, solvents, oxidizers, reducers, fluxes, and colorimetric reagents. (From Grant & Hackh's Chemical Dictionary, 5th ed, p301, p499) Indicator,Reagent,Reagents,Indicators,Reagents and Indicators
D009842 Oligopeptides Peptides composed of between two and twelve amino acids. Oligopeptide
D012083 Renin A highly specific (Leu-Leu) endopeptidase that generates ANGIOTENSIN I from its precursor ANGIOTENSINOGEN, leading to a cascade of reactions which elevate BLOOD PRESSURE and increase sodium retention by the kidney in the RENIN-ANGIOTENSIN SYSTEM. The enzyme was formerly listed as EC 3.4.99.19. Angiotensin-Forming Enzyme,Angiotensinogenase,Big Renin,Cryorenin,Inactive Renin,Pre-Prorenin,Preprorenin,Prorenin,Angiotensin Forming Enzyme,Pre Prorenin,Renin, Big,Renin, Inactive
D012084 Renin-Angiotensin System A BLOOD PRESSURE regulating system of interacting components that include RENIN; ANGIOTENSINOGEN; ANGIOTENSIN CONVERTING ENZYME; ANGIOTENSIN I; ANGIOTENSIN II; and angiotensinase. Renin, an enzyme produced in the kidney, acts on angiotensinogen, an alpha-2 globulin produced by the liver, forming ANGIOTENSIN I. Angiotensin-converting enzyme, contained in the lung, acts on angiotensin I in the plasma converting it to ANGIOTENSIN II, an extremely powerful vasoconstrictor. Angiotensin II causes contraction of the arteriolar and renal VASCULAR SMOOTH MUSCLE, leading to retention of salt and water in the KIDNEY and increased arterial blood pressure. In addition, angiotensin II stimulates the release of ALDOSTERONE from the ADRENAL CORTEX, which in turn also increases salt and water retention in the kidney. Angiotensin-converting enzyme also breaks down BRADYKININ, a powerful vasodilator and component of the KALLIKREIN-KININ SYSTEM. Renin-Angiotensin-Aldosterone System,Renin Angiotensin Aldosterone System,Renin Angiotensin System,System, Renin-Angiotensin,System, Renin-Angiotensin-Aldosterone
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000809 Angiotensins Oligopeptides which are important in the regulation of blood pressure (VASOCONSTRICTION) and fluid homeostasis via the RENIN-ANGIOTENSIN SYSTEM. These include angiotensins derived naturally from precursor ANGIOTENSINOGEN, and those synthesized. Angiotensin
D013329 Structure-Activity Relationship The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups. Relationship, Structure-Activity,Relationships, Structure-Activity,Structure Activity Relationship,Structure-Activity Relationships

Related Publications

J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Difluorostatine- and difluorostatone-containing peptides as potent and specific renin inhibitors.
November 1985, Journal of medicinal chemistry,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Highly potent and specific inhibitors of human renin.
February 1984, Biochemical and biophysical research communications,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Highly potent and specific inhibitors of human renin.
August 1987, FEBS letters,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Highly potent and specific inhibitors of human renin.
January 1985, Hypertension (Dallas, Tex. : 1979),
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Renin inhibition by synthetic peptides related to mouse and human renin prosegments.
December 1984, Journal of hypertension. Supplement : official journal of the International Society of Hypertension,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
[Renin inhibition by peptides and pseudo-peptides].
January 1989, Nephrologie,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Renin inhibition: immunological procedures and renin inhibitor peptides.
January 1989, Fundamental & clinical pharmacology,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Renin inhibition: immunological procedures and renin inhibitor peptides.
October 1988, Kidney international. Supplement,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
Renin: inhibition by proteins and peptides.
July 1974, Biochemistry,
J R Luly, and J J Plattner, and H Stein, and N Yi, and J Soderquist, and P A Marcotte, and H D Kleinert, and T J Perun
New modified heterocyclic phenylalanine derivatives. Incorporation into potent inhibitors of human renin.
March 1992, Journal of medicinal chemistry,
Copied contents to your clipboard!