5 results match your criteria: "The University of Edinburgh School of Chemistry[Affiliation]"

Erratum to "Optical Detection of Distal Lung Enzyme Activity in Human Inflammatory Lung Disease".

BME Front

September 2023

Translational Healthcare Technologies Group, Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, 47 Little France Crescent, Edinburgh BioQuarter, Edinburgh EH16 4TJ, UK.

[This corrects the article DOI: 10.34133/2021/9834163.].

View Article and Find Full Text PDF

Fibroblast Activation Protein Specific Optical Imaging in Non-Small Cell Lung Cancer.

Front Oncol

March 2022

Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, Edinburgh, United Kingdom.

Fibroblast activation protein (FAP) is a cell surface propyl-specific serine protease involved in the regulation of extracellular matrix. Whilst expressed at low levels in healthy tissue, upregulation of FAP on fibroblasts can be found in several solid organ malignancies, including non-small cell lung cancer, and chronic inflammatory conditions such as pulmonary fibrosis and rheumatoid arthritis. Their full role remains unclear, but FAP expressing cancer associated fibroblasts (CAFs) have been found to relate to a poor prognosis with worse survival rates in breast, colorectal, pancreatic, and non-small cell lung cancer (NSCLC).

View Article and Find Full Text PDF

Optical Detection of Distal Lung Enzyme Activity in Human Inflammatory Lung Disease.

BME Front

April 2021

Translational Healthcare Technologies Group, Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, 47 Little France Crescent, Edinburgh BioQuarter, Edinburgh, UK, EH16 4TJ.

There is a need to develop platforms delineating inflammatory biology of the distal human lung. We describe a platform technology approach to detect enzyme activity and observe drug inhibition in the distal human lung using a combination of matrix metalloproteinase (MMP) optical reporters, fibered confocal fluorescence microscopy (FCFM), and a bespoke delivery device. .

View Article and Find Full Text PDF

Enhanced avidity from a multivalent fluorescent antimicrobial peptide enables pathogen detection in a human lung model.

Sci Rep

June 2019

EPSRC IRC PROTEUS Hub, Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, Edinburgh BioQuarter, 47 Little France Crescent, Edinburgh, EH16 4TJ, United Kingdom.

Rapid in situ detection of pathogens coupled with high resolution imaging in the distal human lung has the potential to provide new insights and diagnostic utility in patients in whom pneumonia is suspected. We have previously described an antimicrobial peptide (AMP) Ubiquicidin (fragment UBI) labelled with an environmentally sensitive fluorophore that optically detected bacteria in vitro but not ex vivo. Here, we describe further chemical development of this compound and demonstrate that altering the secondary structure of the AMP to generate a tri-branched dendrimeric scaffold provides enhanced signal in vitro and ex vivo and consequently allows the rapid detection of pathogens in situ in an explanted human lung.

View Article and Find Full Text PDF

A labelled-ubiquicidin antimicrobial peptide for immediate optical detection of live bacteria in human alveolar lung tissue.

Chem Sci

December 2015

Pulmonary Optical Molecular Imaging Group , MRC Centre for Inflammation Research , Queen's Medical Research Institute, 47 Little France Crescent , Edinburgh , EH16 4TJ , UK . Email:

The immediate detection of the presence of bacteria in the distal human lung is of significant clinical utility. Herein we describe the development and optimization of a bacterial binding fragment (UBI) of the antimicrobial peptide, ubiquicidin (UBI), conjugated to an environmentally sensitive fluorophore to enable rapid live bacterial imaging within human lung tissue. UBI was modified for stability in the presence of human lung bronchoalveolar lavage fluid, for affinity to bacterial membranes and functionality in human lung tissue.

View Article and Find Full Text PDF