Home / Publications / Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2

Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2

Mariya Grigor'evna Khrenova 1, 2
Mariya Grigor'evna Khrenova
, 
Ilya Dmitrievich Solovyev 1, 2
Ilya Dmitrievich Solovyev
, 
Viatcheslav Nikolaevich Azev 3
Viatcheslav Nikolaevich Azev
, 
Grigory D Lapshin 2
Grigory D Lapshin
, 
Alexander Pavlovich Savitsky 2
Alexander Pavlovich Savitsky
10.1016/j.mencom.2016.04.009
Published 2016-04-28
Communication , Volume 26, Issue 3, 207-208
1
Share
Cite this
GOST
 | 
Cite this
GOST Copy
Khrenova M. G. et al. Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2 // Mendeleev Communications. 2016. Vol. 26. No. 3. pp. 207-208.
GOST all authors (up to 50) Copy
Khrenova M. G., Solovyev I. D., Azev V. N., Lapshin G. D., Savitsky A. P. Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2 // Mendeleev Communications. 2016. Vol. 26. No. 3. pp. 207-208.
RIS
 | 
Cite this
RIS Copy
TY - JOUR
DO - 10.1016/j.mencom.2016.04.009
UR - https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.04.009
TI - Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2
T2 - Mendeleev Communications
AU - Khrenova, Mariya Grigor'evna
AU - Solovyev, Ilya Dmitrievich
AU - Azev, Viatcheslav Nikolaevich
AU - Lapshin, Grigory D
AU - Savitsky, Alexander Pavlovich
PY - 2016
DA - 2016/04/28
PB - Mendeleev Communications
SP - 207-208
IS - 3
VL - 26
ER -
BibTex
 | 
Cite this
BibTex (up to 50 authors) Copy
@article{2016_Khrenova,
author = {Mariya Grigor'evna Khrenova and Ilya Dmitrievich Solovyev and Viatcheslav Nikolaevich Azev and Grigory D Lapshin and Alexander Pavlovich Savitsky},
title = {Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2},
journal = {Mendeleev Communications},
year = {2016},
volume = {26},
publisher = {Mendeleev Communications},
month = {Apr},
url = {https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.04.009},
number = {3},
pages = {207--208},
doi = {10.1016/j.mencom.2016.04.009}
}
MLA
Cite this
MLA Copy
Khrenova, Mariya Grigor'evna, et al. “Oxoethylene derivative of the natural substrate as an inhibitor of matrix metalloproteinase MMP-2.” Mendeleev Communications, vol. 26, no. 3, Apr. 2016, pp. 207-208. https://mendcomm.colab.ws/publications/10.1016/j.mencom.2016.04.009.

Abstract

A mimetic of a natural substrate of the matrix metalloproteinase MMP-2, in which the amide group with the scissile peptide bond is replaced with the oxoethylene moiety, inhibits the enzyme.

References

1.
Matrix Metalloproteinase Inhibitors. Specificity of Binding and Structure–Activity Relationships, ed. S. P. Gupta, Springer, Basel, 2012.
2.
Matrix Metalloproteinase Inhibitors
Dormán G., Cseh S., Hajdú I., Barna L., Kónya D., Kupai K., Kovács L., Ferdinandy P.
Drugs, 2010
3.
Is there new hope for therapeutic matrix metalloproteinase inhibition?
Vandenbroucke R.E., Libert C.
Nature Reviews Drug Discovery, 2014
4.
Matrix metalloproteinases: a tail of a frog that became a prince
Brinckerhoff C.E., Matrisian L.M.
Nature Reviews Molecular Cell Biology, 2002
5.
Peptide-Based Selective Inhibitors of Matrix Metalloproteinase-Mediated Activities
Ndinguri M., Bhowmick M., Tokmina-Roszyk D., Robichaud T., Fields G.
Molecules, 2012
7.
Structural Basis for Matrix Metalloproteinase-2 (MMP-2)-selective Inhibitory Action of β-Amyloid Precursor Protein-derived Inhibitor
Hashimoto H., Takeuchi T., Komatsu K., Miyazaki K., Sato M., Higashi S.
Journal of Biological Chemistry, 2011
8.
Computational characterization of ketone-ketal transformations at the active site of matrix metalloproteinases
Khrenova M.G., Nemukhin A.V., Savitsky A.P.
Journal of Physical Chemistry B, 2014
9.
Continuously recording fluorescent assays optimized for five human matrix metalloproteinases
Netzel-Arnett S., Mallya S.K., Nagase H., Birkedal-Hansen H., Van Wart H.E.
Analytical Biochemistry, 1991
11.
Studies on sensitivity to racemization of activated residues in couplings of N-benzyloxycarbonyldipeptides
BENOITON N.L., LEE Y.C., STEINAUR R., CHEN F.M.
International journal of peptide & protein research, 2009
12.
Synthesis of keto-methylene and dehydro-keto-methylene pseudo-dipeptides
EWENSON A., COHEN-SUISSA R., LEVIAN-TEITELBAUM D., SELINGER Z., CHOREV M., GILON C.
International journal of peptide & protein research, 2009