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peptide-based selective inhibitors of matrix metalloproteinase-mediated activities肽链型矩阵的选择性抑制剂metalloproteinase-mediated活动.pdf

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peptide-based selective inhibitors of matrix metalloproteinase-mediated activities肽链型矩阵的选择性抑制剂metalloproteinase-mediated活动

Molecules 2012, 17, 14230-14248; doi:10.3390/molecules171214230 OPEN ACCESS molecules ISSN 1420-3049 /journal/molecules Article Peptide-Based Selective Inhibitors of Matrix Metalloproteinase-Mediated Activities Margaret W. Ndinguri 1,2, Manishabrata Bhowmick 1, Dorota Tokmina-Roszyk 1, Trista K. Robichaud 3,4 and Gregg B. Fields 1,4,* 1 Torrey Pines Institute for Molecular Studies, 11350 SW Village Parkway, Port St. Lucie, FL 34987, USA 2 Department of Chemistry, Eastern Kentucky University, 521 Lancaster Avenue, Richmond, KY 40475, USA 3 Department of Periodontics, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA 4 Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA * Author to whom correspondence should be addressed; E-Mail: gfields@; Tel.: +1-772-345-4724; Fax: +1-772-345-3647. Received: 8 October 2012; in revised form: 20 November 2012 / Accepted: 28 November 2012 / Published: 30 November 2012 Abstract: The matrix metalloproteinases (MMPs) exhibit a broad array of activities, some catalytic and some non-catalytic in nature. An overall lack of selectivity has rendered small molecule, active site targeted MMP inhibitors problematic in execution. Inhibitors that favor few or individual members of the MMP family often take advantage of interactions outside the enzyme active site. We presently focus on peptide-based MMP inhibitors and probes that do not incorporate conventional Zn2+ binding gro