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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

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Related Experiment Video

Updated: Jun 12, 2026

Mitigation of Blood Borne Cell Attachment to Metal Implants through CD47-Derived Peptide Immobilization
08:13

Mitigation of Blood Borne Cell Attachment to Metal Implants through CD47-Derived Peptide Immobilization

Published on: December 3, 2020

Metalloproteinase binding proteins: WO2009097397.

Yoshifumi Itoh1

  • 1Kennedy Institute of Rheumatology, Imperial College London, Hammersmith, UK. y.itoh@imperial.ac.uk

Expert Opinion on Therapeutic Patents
|May 22, 2010
PubMed
Summary

Developing selective antibody inhibitors targeting matrix metalloproteinases (MMPs), specifically MMP-14, offers a promising therapeutic strategy for diseases like cancer by inhibiting uncontrolled cell invasion and tissue destruction.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Matrix metalloproteinases (MMPs) are crucial for extracellular matrix (ECM) remodeling.
  • Dysregulated ECM catabolism by MMPs is linked to diseases, notably cancer and arthritis.
  • Previous broad-spectrum MMP inhibitors faced clinical trial failures, necessitating targeted therapeutic approaches.

Purpose of the Study:

  • To explore biologic inhibitors, specifically antibodies, as a therapeutic strategy against MMPs.
  • To develop a selective inhibitor targeting membrane-type 1 MMP (MMP-14).
  • To assess the therapeutic potential of an anti-MMP-14 antibody in preclinical cancer models.

Main Methods:

  • Generation of a selective antibody targeting MMP-14.
  • Characterization of the antibody's inhibitory activity (K(i) of 0.6 nM).

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  • Evaluation of the antibody's efficacy in suppressing tumor growth in mouse models.

    • Main Results:

    • A highly selective MMP-14 inhibitory antibody was successfully generated.
    • The antibody demonstrated potent inhibition with a low nanomolar affinity.
    • Significant suppression of tumor growth was observed in preclinical mouse studies.

    Conclusions:

    • Selective antibody-based inhibition of MMP-14 presents a viable therapeutic avenue.
    • This approach may address unmet needs in treating diseases characterized by uncontrolled cell invasion and tissue destruction.
    • Further development of MMP-14 antibodies could lead to novel cancer therapies.