Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2009 Aug;3(4):255-64.
doi: 10.2976/1.3132954. Epub 2009 May 22.

Photochemical tools to study dynamic biological processes

Alexandre Specht, Frédéric Bolze, Ziad Omran, Jean-François Nicoud, Maurice Goeldner

Photochemical tools to study dynamic biological processes

Alexandre Specht et al. HFSP J. 2009 Aug.

Abstract

Light-responsive biologically active compounds offer the possibility to study the dynamics of biological processes. Phototriggers and photoswitches have been designed, providing the capability to rapidly cause the initiation of wide range of dynamic biological phenomena. We will discuss, in this article, recent developments in the field of light-triggered chemical tools, specially how two-photon excitation, "caged" fluorophores, and the photoregulation of protein activities in combination with time-resolved x-ray techniques should break new grounds in the understanding of dynamic biological processes.

PubMed Disclaimer

Figures

Figure 1
Figure 1. Photoregulation of functional proteins using a phototrigger or a photoswitch.
Figure 2
Figure 2. Several photolabile groups used for the caging of biologically active compounds (LG=leaving group).
Figure 3
Figure 3. (a) Two-photon versus one-photon processes.
(b) Fluorescence localization in one-photon (all light pathway) and two-photon (focal point) excitation of an organic fluorophore (Hayek et al., 2006) (c) Dissymmetric donor-acceptor (CDNI-Glu) and symmetric acceptor-acceptor (BNSF-Glu) caged glutamates with high two-photon uncaging action cross sections.
Figure 4
Figure 4. Cellular protein trafficking studies using caged fluorophores and small genetically encoded peptide tags.
Figure 5
Figure 5. Proposed mechanism for the photoregulation of transporter protein activity using photocleavable crosslinkers.
This class of membrane proteins needs to undergo an important structural rearrangement to catalyze the transport of specific molecules or ions across membrane bilayer. Therefore, they could be locked in one conformation by using both site-directed double cysteine mutants of the protein and intramolecular crosslinking. The UV photolysis of such modified transporters should rapidly and efficiently cleave the crosslinker, leading to the triggering of their activities.
See this image and copyright information in PMC

References

    1. Abramson, J, Smirnova, I, Kasho, V, Verner, G, Kaback, H R, and Iwata, S (2003). “Structure and mechanism of the lactose permease of Escherichia coli.” Science SCIEAS 301(5633), 610–615.10.1126/science.1088196 - DOI - PubMed
    1. Adams, S R, Kao, J PY, Grynkiewicz, G, Minta, A, and Tsien, R Y (1988). “Biologically useful chelators that release Ca2+ upon illumination.” J. Am. Chem. Soc. JACSAT 110(10), 3212–3220.10.1021/ja00218a034 - DOI
    1. Adams, S R, and Tsien, R Y (1993). “Controlling cell chemistry with caged compounds.” Annu. Rev. Physiol. ARPHAD 55, 755–784.10.1146/annurev.ph.55.030193.003543 - DOI - PubMed
    1. Albota, M, et al. (1998). “Design of organic molecules with large two-photon absorption cross sections.” Science SCIEAS 281(5383), 1653–1656.10.1126/science.281.5383.1653 - DOI - PubMed
    1. Anderson, S, Srajer, V, Pahl, R, Rajagopal, S, Schotte, F, Anfinrud, P, Wulff, M, and Moffat, K (2004). “Chromophore conformation and the evolution of tertiary structural changes in photoactive yellow protein.” Structure (London) STRUE6 12(6), 1039–1045.10.1016/j.str.2004.04.008 - DOI - PubMed

LinkOut - more resources