TY - JOUR
TI - Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: A structure-activity study
AU - Vassiliou, S.
AU - Mucha, A.
AU - Cuniasse, P.
AU - Georgiadis, D.
AU - Lucet-Levannier, K.
AU - Beau, F.
AU - Kannan, R.
AU - Murphy, G.
AU - Knäuper, V.
AU - Rio, M.-C.
AU - Basset, P.
AU - Yiotakis, A.
AU - Dive, V.
JO - Journal of Medicinal Chemistry
PY - 2021
VL - 42
TODO - 14
SP - 2610-2620
PB - 
SN - 0022-2623, 1520-4804
TODO - 10.1021/jm9900164
TODO - collagenase;  gelatinase a;  gelatinase b;  matrilysin;  matrix metalloproteinase;  matrix metalloproteinase inhibitor;  phosphinic acid derivative;  phosphinic pseudotripeptide;  stromelysin;  tripeptide;  unclassified drug, article;  drug structure;  drug synthesis;  enzyme inhibition;  in vitro study;  reaction analysis;  structure activity relation, Kinetics;  Magnetic Resonance Spectroscopy;  Metalloendopeptidases;  Oligopeptides;  Phosphines;  Protease Inhibitors;  Structure-Activity Relationship
TODO - Several phosphinic pseudo-tripeptides of general formula R-XaaΨ(PO2- CH2)Xaa'-Yaa'-NH2 were synthesized and evaluated for their in vitro activities to inhibit stromelysin-3, gelatinases A and B, membrane type-1 matrix metalloproteinase, collagenases 1 and 2, and matrilysin. With the exception of collagenase-1 and matrilysin, phosphinic pseudo-tripeptides behave as highly potent inhibitors of matrix metalloproteinases, provided they contain in P1' position an unusual long aryl-alkyl substituent. Study of structure-activity relationships regarding the influence of the R and Xaa' substituents in this series may contribute to the design of inhibitors able to block only a few members of the matrix metalloproteinase family.
ER -