Enrico Gratton

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Enrico Gratton (born 1946) is an Italian-American biophysicist. His research is focused on the field of biophotonics and fluorescence spectroscopy.

Contents

Early life and education

Enrico Gratton completed his graduate studies at the University of Rome, working on a physics thesis related to DNA molecules, chromosomes. [1] From 1969 to 1971 he was a post-doctoral fellow at the Istituto Superiore di Sanità in Italy. [2]

Career

In 1978 Gratton worked as a postdoc with Gregorio Weber at the University of Illinois at Urbana-Champaign, studying protein dynamics. In 1978 he was appointed assistant professor in the Department of Physics at UIUC. In 1989 he was promoted to professor. At Illinois, Gratton established the Laboratory for Fluorescence Dynamics (LFD) in 1986 with long-term funding from the NIH, bringing advanced microscopy and spectroscopy techniques to the study of biological systems. [1] [2]

In 2006, Gratton retired from the University of Illinois and moved his laboratory to the University of California, Irvine, where he was made professor of Biomedical Engineering with joint appointments in biology and physics until his retirement in November of 2023. [3]

Laboratory of Fluorescence Dynamics

In 1986, the National Institutes of Health awarded a grant to Gratton, to establish the Laboratory for Fluorescence Dynamics (LFD), the first national facility dedicated to fluorescence spectroscopy. The LFD is a fluorescence laboratory that serves local, national, and international scientists. The LFD gained international recognition for its development of instrumentation for time-resolved fluorescence spectroscopy using frequency domain methods. [4]

At the LFD, scientists use fluorescence to study cellular processes, including protein aggregation, membrane interactions, and migration of cells, to track moving particles, and to analyze collagen formation and deformation. [5]

Research contributions

Phasor approach is a model-free analysis method used in fluorescence lifetime imaging to map cellular metabolism. This technique has been widely adopted for investigating cellular processes and protein dynamics. [6]

Fluorescence Correlation Spectroscopy (FCS) is a technique used to measure the diffusion and interaction of fluorescently labeled molecules in solution. [7]

Fluorescence Recovery After Photobleaching (FRAP) helps measure dynamics and mobility of molecules within complex biological systems. [8]

Two-photon microscopy allows for noninvasive, three-dimensional imaging of live cells and tissues with reduced phototoxicity. This technology enables the study of cellular and tissue dynamics in intact, living organisms. [9]

Fluorescence Lifetime Imaging (FLIM) is a technique that provides information about the local environment of fluorescent probes and can be used to study various biological parameters such as protein-protein interactions, pH, and ion concentrations. [10]

Awards and recognition

Related Research Articles

<span class="mw-page-title-main">Biophysics</span> Study of biological systems using methods from the physical sciences

Biophysics is an interdisciplinary science that applies approaches and methods traditionally used in physics to study biological phenomena. Biophysics covers all scales of biological organization, from molecular to organismic and populations. Biophysical research shares significant overlap with biochemistry, molecular biology, physical chemistry, physiology, nanotechnology, bioengineering, computational biology, biomechanics, developmental biology and systems biology.

<span class="mw-page-title-main">Förster resonance energy transfer</span> Photochemical energy transfer mechanism

Förster resonance energy transfer (FRET), fluorescence resonance energy transfer, resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores). A donor chromophore, initially in its electronic excited state, may transfer energy to an acceptor chromophore through nonradiative dipole–dipole coupling. The efficiency of this energy transfer is inversely proportional to the sixth power of the distance between donor and acceptor, making FRET extremely sensitive to small changes in distance.

Fluorescence-lifetime imaging microscopy or FLIM is an imaging technique based on the differences in the exponential decay rate of the photon emission of a fluorophore from a sample. It can be used as an imaging technique in confocal microscopy, two-photon excitation microscopy, and multiphoton tomography.

<span class="mw-page-title-main">Max Planck Institute of Biochemistry</span> Research institute in Martinsried, Germany

The Max Planck Institute of Biochemistry is a research institute of the Max Planck Society located in Martinsried, a suburb of Munich. The institute was founded in 1973 by the merger of three formerly independent institutes: the Max Planck Institute of Biochemistry, the Max Planck Institute of Protein and Leather Research, and the Max Planck Institute of Cell Chemistry.

<span class="mw-page-title-main">Max Planck Institute for Biophysical Chemistry</span> Research institute

The Max Planck Institute for Biophysical Chemistry, also known as the Karl-Friedrich Bonhoeffer Institute, was a research institute of the Max Planck Society, located in Göttingen, Germany. On January 1, 2022, the institute merged with the Max Planck Institute for Experimental Medicine in Göttingen to form the Max Planck Institute for Multidisciplinary Sciences.

Fluorescence correlation spectroscopy (FCS) is a statistical analysis, via time correlation, of stationary fluctuations of the fluorescence intensity. Its theoretical underpinning originated from L. Onsager's regression hypothesis. The analysis provides kinetic parameters of the physical processes underlying the fluctuations. One of the interesting applications of this is an analysis of the concentration fluctuations of fluorescent particles (molecules) in solution. In this application, the fluorescence emitted from a very tiny space in solution containing a small number of fluorescent particles (molecules) is observed. The fluorescence intensity is fluctuating due to Brownian motion of the particles. In other words, the number of the particles in the sub-space defined by the optical system is randomly changing around the average number. The analysis gives the average number of fluorescent particles and average diffusion time, when the particle is passing through the space. Eventually, both the concentration and size of the particle (molecule) are determined. Both parameters are important in biochemical research, biophysics, and chemistry.

<span class="mw-page-title-main">Molecular biophysics</span> Interdisciplinary research area

Molecular biophysics is a rapidly evolving interdisciplinary area of research that combines concepts in physics, chemistry, engineering, mathematics and biology. It seeks to understand biomolecular systems and explain biological function in terms of molecular structure, structural organization, and dynamic behaviour at various levels of complexity. This discipline covers topics such as the measurement of molecular forces, molecular associations, allosteric interactions, Brownian motion, and cable theory. Additional areas of study can be found on Outline of Biophysics. The discipline has required development of specialized equipment and procedures capable of imaging and manipulating minute living structures, as well as novel experimental approaches.

Watt Wetmore Webb was an American biophysicist, known for his co-invention of multiphoton microscopy in 1990.

Chemical imaging is the analytical capability to create a visual image of components distribution from simultaneous measurement of spectra and spatial, time information. Hyperspectral imaging measures contiguous spectral bands, as opposed to multispectral imaging which measures spaced spectral bands.

In biology, membrane fluidity refers to the viscosity of the lipid bilayer of a cell membrane or a synthetic lipid membrane. Lipid packing can influence the fluidity of the membrane. Viscosity of the membrane can affect the rotation and diffusion of proteins and other bio-molecules within the membrane, there-by affecting the functions of these things.

Fluorescence cross-correlation spectroscopy (FCCS) is a spectroscopic technique that examines the interactions of fluorescent particles of different colours as they randomly diffuse through a microscopic detection volume over time, under steady conditions.

A model lipid bilayer is any bilayer assembled in vitro, as opposed to the bilayer of natural cell membranes or covering various sub-cellular structures like the nucleus. They are used to study the fundamental properties of biological membranes in a simplified and well-controlled environment, and increasingly in bottom-up synthetic biology for the construction of artificial cells. A model bilayer can be made with either synthetic or natural lipids. The simplest model systems contain only a single pure synthetic lipid. More physiologically relevant model bilayers can be made with mixtures of several synthetic or natural lipids.

<span class="mw-page-title-main">Fluorescence in the life sciences</span> Scientific investigative technique

Fluorescence is used in the life sciences generally as a non-destructive way of tracking or analysing biological molecules. Some proteins or small molecules in cells are naturally fluorescent, which is called intrinsic fluorescence or autofluorescence. The intrinsic DNA fluorescence is very weak.Alternatively, specific or general proteins, nucleic acids, lipids or small molecules can be "labelled" with an extrinsic fluorophore, a fluorescent dye which can be a small molecule, protein or quantum dot. Several techniques exist to exploit additional properties of fluorophores, such as fluorescence resonance energy transfer, where the energy is passed non-radiatively to a particular neighbouring dye, allowing proximity or protein activation to be detected; another is the change in properties, such as intensity, of certain dyes depending on their environment allowing their use in structural studies.

The following outline is provided as an overview of and topical guide to biophysics:

<span class="mw-page-title-main">Macromolecular assembly</span> Large chemical complexes composed of polymers and other macromolecules

In molecular biology, the term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially, and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things, and are composed of many hundreds or thousands of atoms held together by covalent bonds; they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic, though the MA term is more commonly applied in biology, and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions, and can be in either non-repeating structures, or in repeating linear, circular, spiral, or other patterns. The process by which MAs are formed has been termed molecular self-assembly, a term especially applied in non-biologic contexts. A wide variety of physical/biophysical, chemical/biochemical, and computational methods exist for the study of MA; given the scale of MAs, efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.

<span class="mw-page-title-main">Laurdan</span> Chemical compound

Laurdan is an organic compound which is used as a fluorescent dye when applied to fluorescence microscopy. It is used to investigate membrane qualities of the phospholipid bilayers of cell membranes. One of its most important characteristics is its sensitivity to membrane phase transitions as well as other alterations to membrane fluidity such as the penetration of water.

Pump–probe microscopy is a non-linear optical imaging modality used in femtochemistry to study chemical reactions. It generates high-contrast images from endogenous non-fluorescent targets. It has numerous applications, including materials science, medicine, and art restoration.

Laura Marcu is an American scientist and a professor of biomedical engineering and neurological surgery at the University of California, Davis. She is also a Fellow of numerous professional societies: the Biomedical Engineering Society, SPIE, The Optical Society and the National Academy of Inventors.

Gerd Ulrich "Uli" Nienhaus is a German physicist who is a professor and director of the Institute of Applied Physics, Karlsruhe Institute of Technology (KIT). At the KIT, he is also affiliated with the Institute of Nanotechnology, Institute of Biological and Chemical Systems, and Institute of Physical Chemistry, and he is an adjunct professor at the University of Illinois at Urbana-Champaign.

Michelle Digman is an American chemist who is an associate professor at the University of California, Irvine. She is Director of W.M. Keck Nanoimaging Lab and co-leads the Laboratory for Fluorescence Dynamics. Her research develops imaging technologies to better understand biological problems.

References

  1. 1 2 "Enrico Gratton". 14 January 2022.
  2. 1 2 "Instructors - Genova2004 - Instructors - the Fluorescence Foundation".
  3. ↑ "UCI hires prominent physicist". 22 February 2006.
  4. ↑ Gratton, Enrico. "Laboratory for Fluorescence Dynamics" – via grantome.com.{{cite journal}}: Cite journal requires |journal= (help)
  5. ↑ "Enrico Gratton (University of California, Irvine) | J. Heyrovsky Institute of Physical Chemistry".
  6. ↑ Malacrida, Leonel; Gratton, Enrico; Jameson, David M. (December 7, 2015). "Model-free methods to study membrane environmental probes: a comparison of the spectral phasor and generalized polarization approaches". Methods and Applications in Fluorescence. 3 (4): 047001. doi:10.1088/2050-6120/3/4/047001. PMC   4862737 . PMID   27182438.
  7. ↑ "[4] Fluorescence correlation spectroscopy - ScienceDirect". doi:10.1016/S0076-6879(03)61006-2.
  8. ↑ Sanchez, S., Tricerri, M., & Gratton, E. (2007). Interaction of high-density lipoprotein particles with membranes containing cholesterol. The Journal of Lipid Research, 48(8), 1689-1700. https://doi.org/10.1194/jlr.m600457-jlr200
  9. ↑ Gratton, Enrico; Breusegem, Sophie; Sutin, Jason; Ruan, Qiaoqiao; Barry, Nicholas (July 7, 2003). "Fluorescence lifetime imaging for the two-photon microscope: time-domain and frequency-domain methods". Journal of Biomedical Optics. 8 (3): 381–390. doi:10.1117/1.1586704. PMID   12880343 – via PubMed.
  10. ↑ Scipioni, Lorenzo; Rossetta, Alessandro; Tedeschi, Giulia; Gratton, Enrico (May 7, 2021). "Phasor S-FLIM: a new paradigm for fast and robust spectral fluorescence lifetime imaging". Nature Methods. 18 (5): 542–550. doi:10.1038/s41592-021-01108-4. PMC   10161785 . PMID   33859440.
  11. ↑ "APS Fellow Archive". www.aps.org.
  12. ↑ "Past Council | Biophysical Society". www.biophysics.org.
  13. ↑ "Fellow Directory - AIMBE".
  14. ↑ "Enrico Gratton Recognized with Honorary Doctorate in Uruguay | Samueli School of Engineering at UC Irvine".
  15. ↑ "Enrico Gratton: The 2021 SPIE Britton Chance Biomedical Optics Award".
  16. ↑ "Enrico Gratton to Receive 2019 BPS Avanti Award in Lipids".
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