Abstract
Molecular imaging requires the highest possible signal-to-noise ratios (SNRs) at the target of interest. In order to maximize the SNR for optical imaging techniques, various strategies have been developed to design fluorescent probes that can be activated, for example, by proteolytic degradation. Generally speaking, these probes are quenched in their native state—e.g., by fluorescence resonance energy transfer (FRET)—and dequenched after cleavage or hybridization, which is associated with a strong fluorescence signal increase.
Different strategies of fluorescence signal amplification ranging from large and small protease-sensing molecules to oligonucleotide-sensing and nanoparticle-based probes are presented in this chapter.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Aparicio T, Kermorgant S, Dessirier V, Lewin MJ, Lehy T (1999) Matrix metalloproteinase inhibition prevents colon cancer peritoneal carcinomatosis development and prolongs survival in rats. Carcinogenesis 20:1445–1451
Bremer C, Ntziachristos V, Weissleder R (2003) Optical-based molecular imaging: contrast agents and potential medical applications. Eur Radiol 13:231–243
Bremer C, Ntziachristos V, Weitkamp B, Theilmeier G, Heindel W, Weissleder R (2005) Optical imaging of spontaneous breast tumors using protease sensing ‘smart’ optical probes. Invest Radiol 40:321–327
Bremer C, Tung CH, Bogdanov A Jr, Weissleder R (2002) Imaging of differential protease expression in breast cancers for detection of aggressive tumor phenotypes. Radiology 222:814–818
Bremer C, Tung CH, Weissleder R (2002) Molecular imaging of MMP expression and therapeutic MMP inhibition. Acad Radiol 9(Suppl 2):S314–S315
Bullok K, Piwnica-Worms D (2005) Synthesis and characterization of a small, membrane-permeant, caspase-activatable far-red fluorescent peptide for imaging apoptosis. J Med Chem 48:5404–5407
Chen J, Tung CH, Mahmood U, Ntziachristos V, Gyurko R, Fishman MC, Huang PL, Weissleder R (2002) In vivo imaging of proteolytic activity in atherosclerosis. Circulation 105:2766–2771
Dubertret B, Calame M, Libchaber AJ (2001) Single-mismatch detection using gold-quenched fluorescent oligonucleotides. Nat Biotechnol 19:365–370
Edwards DR, Murphy G (1998) Cancer. Proteases–invasion and more. Nature 394:527–528
Fang J, Shing Y, Wiederschain D, Yan L, Butterfield C, Jackson G, Harper J, Tamvakopoulos G, Moses MA (2000) Matrix metalloproteinase-2 is required for the switch to the angiogenic phenotype in a tumor model. Proc Natl Acad Sci USA 97:3884–3889
Folkman J (1999) Angiogenic zip code. Nat Biotechnol 17:749
Herszenyi L, Plebani M, Carraro P, De Paoli M, Roveroni G, Cardin R, Tulassay Z, Naccarato R, Farinati F (1999) The role of cysteine and serine proteases in colorectal carcinoma. Cancer 86:1135–1142
Jaffer FA, Tung CH, Wykrzykowska JJ, Ho NH, Houng AK, Reed GL, Weissleder R (2004) Molecular imaging of factor XIIIa activity in thrombosis using a novel, near-infrared fluorescent contrast agent that covalently links to thrombi. Circulation 110:170–176
Jiang T, Olson ES, Nguyen QT, Roy M, Jennings PA, Tsien RY (2004) Tumor imaging by means of proteolytic activation of cell-penetrating peptides. Proc Natl Acad Sci USA 101:17867–17872
Josephson L, Kircher MF, Mahmood U, Tang Y, Weissleder R (2002) Near-infrared fluorescent nanoparticles as combined MR/optical imaging probes. Bioconjug Chem 13:554–560
Kim DE, Schellingerhout D, Jaffer FA, Weissleder R, Tung CH (2005) Near-infrared fluorescent imaging of cerebral thrombi and blood-brain barrier disruption in a mouse model of cerebral venous sinus thrombosis. J Cereb Blood Flow Metab 25:226–233
Kircher MF, Mahmood U, King RS, Weissleder R, Josephson L (2003) A multimodal nanoparticle for preoperative magnetic resonance imaging and intraoperative optical brain tumor delineation. Cancer Res 63:8122–8125
Koblinski JE, Ahram M, Sloane BF (2000) Unraveling the role of proteases in cancer. Clin Chim Acta 291:113–135
Law B, Weissleder R, Tung CH (2005) Mechanism-based fluorescent reporter for protein kinase A detection. Chembiochem 6:1361–1367
Messerli SM, Prabhakar S, Tang Y, Shah K, Cortes ML, Murthy V, Weissleder R, Breakefield XO, Tung CH (2004) A novel method for imaging apoptosis using a caspase-1 near-infrared fluorescent probe. Neoplasia 6:95–105
Metelev V, Weissleder R, Bogdanov A, Jr. (2004) Synthesis and properties of fluorescent NF-kappa B-recognizing hairpin oligodeoxyribonucleotide decoys. Bioconjug Chem 15:1481–1487
Pham W, Choi Y, Weissleder R, Tung CH (2004) Developing a peptide-based near-infrared molecular probe for protease sensing. Bioconjug Chem 15:1403–1407
Pham W, Weissleder R, Tung CH (2002) An azulene dimer as a near-infrared quencher. Angew Chem Int Ed Engl 41:3659–3662, 3519
Schellenberger EA, Sosnovik D, Weissleder R, Josephson L (2004) Magneto/optical annexin V, a multimodal protein. Bioconjug Chem 15:1062–1067
Tung CH, Mahmood U, Bredow S, Weissleder R (2000) In vivo imaging of proteolytic enzyme activity using a novel molecular reporter. Cancer Res 60:4953–4958
Tung CH, Zeng Q, Shah K, Kim DE, Schellingerhout D, Weissleder R (2004) In vivo imaging of beta-galactosidase activity using far red fluorescent switch. Cancer Res 64:1579–1583
Tyagi S, Marras SA, Kramer FR (2000) Wavelength-shifting molecular beacons. Nat Biotechnol 18:1191–1196
Weissleder R, Tung CH, Mahmood U, Bogdanov A Jr. (1999) In vivo imaging of tumors with protease-activated near-infrared fluorescent probes. Nat Biotechnol 17:375–378
Wunder A, Tung CH, Muller-Ladner U, Weissleder R, Mahmood U (2004) In vivo imaging of protease activity in arthritis: a novel approach for monitoring treatment response. Arthritis Rheum 50:2459–2465
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2008 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Bremer, C. (2008). Optical Methods. In: Semmler, W., Schwaiger, M. (eds) Molecular Imaging II. Handbook of Experimental Pharmacology, vol 185/2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-77496-9_1
Download citation
DOI: https://doi.org/10.1007/978-3-540-77496-9_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-540-77449-5
Online ISBN: 978-3-540-77496-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)