Single-quantum dot imaging with a photon counting camera.

Curr Pharm Biotechnol

Department of Chemistry & Biochemistry, UCLA, Los Angeles, CA, USA.

Published: August 2009

The expanding spectrum of applications of single-molecule fluorescence imaging ranges from fundamental in vitro studies of biomolecular activity to tracking of receptors in live cells. The success of these assays has relied on progress in organic and non-organic fluorescent probe developments as well as improvements in the sensitivity of light detectors. We describe a new type of detector developed with the specific goal of ultra-sensitive single-molecule imaging. It is a wide-field, photon-counting detector providing high temporal and high spatial resolution information for each incoming photon. It can be used as a standard low-light level camera, but also allows access to a lot more information, such as fluorescence lifetime and spatio-temporal correlations. We illustrate the single-molecule imaging performance of our current prototype using quantum dots and discuss on-going and future developments of this detector.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2830710PMC
http://dx.doi.org/10.2174/138920109788922100DOI Listing

Publication Analysis

Top Keywords

single-molecule imaging
8
single-quantum dot
4
imaging
4
dot imaging
4
imaging photon
4
photon counting
4
counting camera
4
camera expanding
4
expanding spectrum
4
spectrum applications
4

Similar Publications

The emerging combination of chemotherapy and radionuclide therapy has been actively investigated to overcome the limitations of monotherapy and augment therapeutic efficacy. However, it remains a challenge to design a single delivery vehicle that can incorporate chemotherapeutics and radionuclides into a compact structure. Here, a chelator DOTA- or NOTA-modified Evans blue conjugated camptothecin molecule (EB-CPT) nanoprodrug was synthesized, which could self-assemble into nanoparticles due to its inherent amphiphilicity.

View Article and Find Full Text PDF

Single-molecule fluorescence resonance energy transfer (smFRET) is a powerful technique for studying the structural dynamics of protein molecules or detecting interactions between protein molecules in real time. Due to the high sensitivity in spatial and temporal resolution, smFRET can decipher sub-populations within heterogeneous native state conformations, which are generally lost in traditional measurements due to ensemble averaging. In addition, the single-molecule reconstitution allows protein molecules to be observed for an extensive period of time and can recapitulate the geometry of the cellular environment to retain biological function.

View Article and Find Full Text PDF

Aims: Establishment of a protocol for routine single-molecule localisation microscopy (SMLM) imaging on formalin fixed paraffin embedded (FFPE) tissue using medical renal disease including minimal change disease (MCD) and focal segmental glomerulosclerosis (FSGS).

Methods: Protocol for normal and diseased renal FFPE tissue was developed to investigate the clinical diagnostic potential of SMLM. Antibody concentrations were determined for confocal microscopy and transferred to SMLM.

View Article and Find Full Text PDF

AGEing of collagen: The effects of glycation on collagen's stability, mechanics and assembly.

Matrix Biol

February 2025

Department of Physics, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada. Electronic address:

Advanced Glycation End Products (AGEs) are the end result of the irreversible, non-enzymatic glycation of proteins by reducing sugars. These chemical modifications accumulate with age and have been associated with various age-related and diabetic complications. AGEs predominantly accumulate on proteins with slow turnover rates, of which collagen is a prime example.

View Article and Find Full Text PDF

Molecular Determinants of Protein Pathogenicity at the Single-Aggregate Level.

Adv Sci (Weinh)

January 2025

Sheffield Institute for Translational Neuroscience, Division of Neuroscience, University of Sheffield, Sheffield, S10 2HQ, UK.

Determining the structure-function relationships of protein aggregates is a fundamental challenge in biology. These aggregates, whether formed in vitro, within cells, or in living organisms, present significant heterogeneity in their molecular features such as size, structure, and composition, making it difficult to determine how their structure influences their functions. Interpreting how these molecular features translate into functional roles is crucial for understanding cellular homeostasis and the pathogenesis of various debilitating diseases like Alzheimer's and Parkinson's.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!