TY - GEN
T1 - Detection of specific binding to HER2 receptors by in vivo fluorescence lifetime imaging
AU - Ardeshirpour, Yasaman
AU - Chernomordik, Victor
AU - Hassan, Moinuddin
AU - Zielinski, Rafal
AU - Griffiths, Gary
AU - Vasalatiy, Olga
AU - Smirnov, Aleksandr V.
AU - Knutson, Jay R.
AU - Achilefu, Samuel
AU - Capala, Jacek
AU - Gandjbakhche, Amir
N1 - Funding Information:
Considerable information concerning the structure of proteins in solution can be obtained from measurement of their optical activity. The great asymmetry of protein molecules is responsible for the large signals they display in the interrelated methods of optical rotatory dispersion (ORD) and circular dichroism (CD). ORD is the measurement, as a function of wavelength, of a molecule's ability to rotate the plane of linearly polarized light; CD is similar data evaluating the molecule's unequal absorption of right-and left-handed circularly polarized light. Although all the amino acids except glycine contain at least one asymmetric carbon atom (the L or D configuration), most amino acids display only small ORD and CD bands. 2 It is the conformation of the protein, that is, the asymmetric and periodic arrangement of peptide units in space, which gives rise to their characteristic ORD and CD spectra. In recent years X-ray diffraction analysis has lead to the complete mapping of the peptide backbone and side-chain positions of lysozyme, 3'4 several other enzymes, 5 and quite a few other proteins~, 7 in the solid state. Newer techniques such as neutron diffraction (for an example, see Schoenborn 8) and high resolution nuclear magnetic resonance (for a 'Contribution No. 869 of the Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02154. This work was supported in part by grants from the U.S. Public Health Service (GM 17533), National Science Foundation (GB 29204X), American Heart Association (71-111), and the American Cancer Society (P-577). N. J. G. is at Merck, Sharp, and Dohme Research Laboratories, Rahway, New Jersey. 2 C. Toniolo, J. Phys. Chem. 74, 1390 (1970). 3 C. C. F. Blake, D. F. Koenig, G. A. Mair, A. C. T. North, D. C. Phillips, and V. R. Sarma, Nature (London) 206, 757 (1965). * D. C. Phillips, Sci. Amer. 215, 78 (1966) ; Proc. Nat. Acad. Sci. U.S. 57, 484 (1967). D. M. Blow and T. A. S~eitz, Annu. Rev. Biochem. 39, 63 (1970). ~D. R. Davies, Annu. Rev. Biochem. 36, 321 (1967). ~R. E. Dickerson and I. Geis, "The Structure and Action of Proteins." Harper, New York, 1969. 8B. P. Schoenborn, Nature (London) 224, 143 (1969).
PY - 2012
Y1 - 2012
N2 - In this study we have shown that in-vivo fluorescence lifetime imaging can be used for early detection of specific probe binding to HER2 receptors, providing information on HER2 overexpression.
AB - In this study we have shown that in-vivo fluorescence lifetime imaging can be used for early detection of specific probe binding to HER2 receptors, providing information on HER2 overexpression.
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U2 - 10.1364/biomed.2012.btu3a.24
DO - 10.1364/biomed.2012.btu3a.24
M3 - Conference contribution
AN - SCOPUS:84890777469
SN - 9781557529428
T3 - Biomedical Optics, BIOMED 2012
SP - BTu3A.24
BT - Biomedical Optics, BIOMED 2012
PB - Optical Society of America (OSA)
T2 - Biomedical Optics, BIOMED 2012
Y2 - 28 April 2012 through 2 May 2012
ER -