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Structure-Energy study of the interactions between matrix metalloproteinase 1 and tissue inhibitor of metalloproteinase

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Date Issued:
2014
Abstract/Description:
Matrix metalloproteinases MMPs are one of the major families of proteinases that play key roles in maintaining an appropriately assembled extracellular matrix ECM. MMPs are essential to many biological processes, such as wound healing, embryo implantation, bone remodeling, and organogenesis. Their biological antagonists, the tissue inhibitors of metalloproteinases TIMPs, regulate the enzymatic activities of MMPs. Uncontrolled ECM degradation occurs when the delicate balance between TIMPs and MMPs is disrupted, resulting in many diseases such as rheumatoid and osteoarthritis, cancer cell metastasis, and heart disease. There are currently no effective treatments for osteoarthritis OA except for joint replacement surgery. Therefore, gaining the knowledge about the structures and molecular mechanisms of these key enzymes in order to uncover new ways to specifically inhibit these proteinases are an opportunity for the development of therapeutics and treatments to prevent the joint destruction seen in OA. Our goal is to understand the biophysical interaction of catalytic domain of MMP-1 with NTIMP- 3 using isothermal calorimetry ITC. The ITC determines if binding between the proteins is entropy or enthalpy driven and heat capacity will indicate the hydrophobic or hydrophilic contributions of the interaction. The information from the ITC results in combination with the known structures of N-TIMP-3/cd_MMP-1 will provide a more complete picture of the interaction. This is in particular of relevance with respect clinical application by engineering TIMPs for targeted inhibition of particular MMPs to treat diseases such as: cancer and arthritis.
Title: Structure-Energy study of the interactions between matrix metalloproteinase 1 and tissue inhibitor of metalloproteinase.
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Name(s): Logue, Timothy
Brew, Keith
Graduate College
Type of Resource: text
Genre: Abstract
Date Created: 2014
Date Issued: 2014
Publisher: Florida Atlantic University
Place of Publication: Boca Raton, Fla.
Physical Form: application/pdf
Extent: 1 p.
Language(s): English
Abstract/Description: Matrix metalloproteinases MMPs are one of the major families of proteinases that play key roles in maintaining an appropriately assembled extracellular matrix ECM. MMPs are essential to many biological processes, such as wound healing, embryo implantation, bone remodeling, and organogenesis. Their biological antagonists, the tissue inhibitors of metalloproteinases TIMPs, regulate the enzymatic activities of MMPs. Uncontrolled ECM degradation occurs when the delicate balance between TIMPs and MMPs is disrupted, resulting in many diseases such as rheumatoid and osteoarthritis, cancer cell metastasis, and heart disease. There are currently no effective treatments for osteoarthritis OA except for joint replacement surgery. Therefore, gaining the knowledge about the structures and molecular mechanisms of these key enzymes in order to uncover new ways to specifically inhibit these proteinases are an opportunity for the development of therapeutics and treatments to prevent the joint destruction seen in OA. Our goal is to understand the biophysical interaction of catalytic domain of MMP-1 with NTIMP- 3 using isothermal calorimetry ITC. The ITC determines if binding between the proteins is entropy or enthalpy driven and heat capacity will indicate the hydrophobic or hydrophilic contributions of the interaction. The information from the ITC results in combination with the known structures of N-TIMP-3/cd_MMP-1 will provide a more complete picture of the interaction. This is in particular of relevance with respect clinical application by engineering TIMPs for targeted inhibition of particular MMPs to treat diseases such as: cancer and arthritis.
Identifier: FA00005833 (IID)
Collection: FAU Student Research Digital Collection
Note(s): The Fifth Annual Graduate Research Day was organized by Florida Atlantic University’s Graduate Student Association. Graduate students from FAU Colleges present abstracts of original research and posters in a competition for monetary prizes, awards, and recognition
Held by: Florida Atlantic University Libraries
Sublocation: Digital Library
Persistent Link to This Record: http://purl.flvc.org/fau/fd/FA00005833
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Host Institution: FAU
Is Part of Series: Florida Atlantic University Digital Library Collections.