Online citations, reference lists, and bibliographies.
← Back to Search

Novel Diphenyl Esters Of Peptidyl α-aminoalkylphosphonates As Inhibitors Of Chymotrypsin And Subtilisin

Ewa Pietrusewicz, M. Sieńczyk, J. Oleksyszyn
Published 2009 · Medicine, Chemistry

Cite This
Download PDF
Analyze on Scholarcy
Share
The activities of novel Cbz-N-protected α-aminophosphonic phenyl esters, analogs of leucine (1–15) and phenylalanine (17–29), which are substituted at the phenyl ester rings, as well as of their peptidic derivatives (31–43), were investigated for their inhibitory effects on chymotrypsin and subtilisin. The chemical nature and position of the examined substituents clearly demonstrated a strong structure–activity relationship. Among all synthesized compounds the most potent phosphonic-type inhibitors of subtilisin and chymotrypsin were identified, with k2/Ki values 114,380 M−1s−1 and 307,380 M−1s−1, respectively.
This paper references
10.3109/14756369409020197
alpha-Aminoalkylphosphonate di(chlorophenyl) esters as inhibitors of serine proteases.
B. Boduszek (1994)
10.1016/0020-711x(90)90244-w
Proteolytic Enzymes: A Practical Approach
R. Beynon (2001)
Inhibition of proteolytic enzymes
GS Salvesen (1989)
10.1016/0006-291X(89)91572-6
Irreversible inhibition of serine proteases by peptidyl derivatives of alpha-aminoalkylphosphonate diphenyl esters.
J. Oleksyszyn (1989)
The characterization of enzyme inhibition
CG Knight (1986)
10.1016/0076-6879(94)44004-2
[2] Families of serine peptidases
N. Rawlings (1994)
10.1021/JM0700619
Discovery of potent, selective, orally active, nonpeptide inhibitors of human mast cell chymase.
M. N. Greco (2007)
10.1021/BI00216A026
Irreversible inhibition of serine proteases by peptide derivatives of (alpha-aminoalkyl)phosphonate diphenyl esters.
J. Oleksyszyn (1991)
10.1021/JM700962J
Small, potent, and selective diaryl phosphonate inhibitors for urokinase-type plasminogen activator with in vivo antimetastatic properties.
J. Joossens (2007)
10.1016/J.EJPHAR.2004.08.040
Therapeutic applications of chymase inhibitors in cardiovascular diseases and fibrosis.
S. Takai (2004)
Families of serine proteases
ND Rawlings (1994)
10.1074/JBC.M501302200
A Novel, Potent Dual Inhibitor of the Leukocyte Proteases Cathepsin G and Chymase
L. de Garavilla (2005)
10.1016/0076-6879(94)44032-8
Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases.
J. Oleksyszyn (1994)
10.1645/GE-622R1.1
CHARACTERIZATION OF SUBTILASE PROTEASE IN CRYPTOSPORIDIUM PARVUM AND C. HOMINIS
X. Feng (2007)



This paper is referenced by
Palladium and Ruthenium Catalyzed Reactions
Bryan E. Jaksic (2011)
10.1016/j.bmcl.2011.01.083
Simple phosphonic inhibitors of human neutrophil elastase.
M. Sieńczyk (2011)
10.3390/ijms20092232
ClpP Protease, a Promising Antimicrobial Target
Carlos Moreno-Cinos (2019)
10.1021/jm300599x
Human neutrophil elastase phosphonic inhibitors with improved potency of action.
Łukasz Winiarski (2012)
10.1039/C5MD00288E
The first potent diphenyl phosphonate KLK4 inhibitors with unexpected binding kinetics
Jeroen Van Soom (2015)
10.1002/9781118299715.CH3
Design and Synthesis of Phosphite Ligands for Homogeneous Catalysis
Aitor Gual (2012)
10.1016/j.bmcl.2012.07.011
The development of first Staphylococcus aureus SplB protease inhibitors: phosphonic analogues of glutamine.
B. Ewa (2012)
10.1016/j.biochi.2014.05.006
Substrate profiling of Finegoldia magna SufA protease, inhibitor screening and application to prevent human fibrinogen degradation and bacteria growth in vitro.
E. Burchacka (2014)
10.1016/J.TETLET.2013.07.049
A convenient method for the one-step synthesis of phosphonic peptides
Marcin Skoreński (2013)
10.1016/j.bmcl.2015.06.039
Discovery of non-competitive thrombin inhibitor derived from competitive tryptase inhibitor skeleton: Shift in molecular recognition resulted from skeletal conversion of carboxylate into phosphonate.
H. Aoyama (2015)
10.1016/J.TETLET.2013.01.039
Efficient methods for the synthesis of α-aminophosphonate fluoroalkyl esters
Marcin Skoreński (2013)
10.1002/cbic.201402360
Synthesis of Novel Phosphonic‐Type Activity‐Based Probes for Neutrophil Serine Proteases and Their Application in Spleen Lysates of Different Organisms
R. Grzywa (2014)
10.1002/pro.2403
Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus
E. Burchacka (2014)
Semantic Scholar Logo Some data provided by SemanticScholar