@article{3023214,
    title = "Phosphinic pseudo-tripeptides as potent inhibitors of matrix metalloproteinases: A structure-activity study",
    author = "Vassiliou, S. and Mucha, A. and Cuniasse, P. and Georgiadis, D. and Lucet-Levannier, K. and Beau, F. and Kannan, R. and Murphy, G. and Knäuper, V. and Rio, M.-C. and Basset, P. and Yiotakis, A. and Dive, V.",
    journal = "Journal of Medicinal Chemistry",
    year = "1999",
    volume = "42",
    number = "14",
    pages = "2610-2620",
    issn = "0022-2623, 1520-4804",
    doi = "10.1021/jm9900164",
    keywords = "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",
    abstract = "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."
}