메뉴 건너뛰기




Volumn 2, Issue 12, 2007, Pages 3201-3209

Tools for investigating peptide-protein interactions: Peptide incorporation of environment-sensitive fluorophores via on-resin derivatization

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOPYRIDINE; 4 DIMETHYLAMINOPYRIDINE; 4-DIMETHYLAMINOPYRIDINE; 6 N,N DIMETHYLAMINO 2,3 NAPHTHALIMIDE; 6-N,N-DIMETHYLAMINO-2,3-NAPHTHALIMIDE; DRUG DERIVATIVE; FLUORESCENT DYE; IMIDE; NAPHTHALENE DERIVATIVE; NAPHTHALIMIDE DERIVATIVE; PEPTIDE; PROTEIN; UNCLASSIFIED DRUG;

EID: 39149125153     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2007.442     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 0344443386 scopus 로고    scopus 로고
    • Versatile fluorescence probes of protein kinase activity
    • Shults, M.D. & Imperiali, B. Versatile fluorescence probes of protein kinase activity. J. Am. Chem. Soc. 125, 14248-14249 (2003).
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 14248-14249
    • Shults, M.D.1    Imperiali, B.2
  • 2
    • 1542298996 scopus 로고    scopus 로고
    • Biosensors of protein kinase action: From in vitro assays to living cells
    • Chen, C.-A., Yeh, R.-H., Yan, X. & Lawrence, D.S. Biosensors of protein kinase action: from in vitro assays to living cells. Biochim. Biophys. Acta 1697, 39-51 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 39-51
    • Chen, C.-A.1    Yeh, R.-H.2    Yan, X.3    Lawrence, D.S.4
  • 3
    • 34247851104 scopus 로고    scopus 로고
    • Seeing is believing: Peptide-based fluorescent sensors of protein tyrosine kinase activity
    • Lawrence, D.S. & Wang, Q. Seeing is believing: peptide-based fluorescent sensors of protein tyrosine kinase activity. Chembiochem 8, 373-378 (2007).
    • (2007) Chembiochem , vol.8 , pp. 373-378
    • Lawrence, D.S.1    Wang, Q.2
  • 4
    • 0030971246 scopus 로고    scopus 로고
    • Fluorescence methods forstudying kinetics of protein-folding reactions
    • Eftink, M.R. & Shastry, M.C. Fluorescence methods forstudying kinetics of protein-folding reactions. Methods Enzymol. 278, 258-286 (1997).
    • (1997) Methods Enzymol , vol.278 , pp. 258-286
    • Eftink, M.R.1    Shastry, M.C.2
  • 5
    • 0036669824 scopus 로고    scopus 로고
    • Measuring protein conformational changes by FRET/LRET
    • Heyduk, T. Measuring protein conformational changes by FRET/LRET. Curr. Opin. Biotechnol. 13, 292-296 (2002).
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 292-296
    • Heyduk, T.1
  • 6
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect proteinprotein interactions and protein conformational changes in vivo
    • Truong, K. & Ikura, M. The use of FRET imaging microscopy to detect proteinprotein interactions and protein conformational changes in vivo. Curr. Opin. Struct. Biol. 11, 573-578 (2001).
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 7
    • 0037279631 scopus 로고    scopus 로고
    • Fluorescence: Basic concepts, practical aspects, and some anecdotes
    • Jameson, D.M., Croney, J.C. & Moens, P.D. Fluorescence: basic concepts, practical aspects, and some anecdotes. Methods Enzymol. 360, 1-43 (2003).
    • (2003) Methods Enzymol , vol.360 , pp. 1-43
    • Jameson, D.M.1    Croney, J.C.2    Moens, P.D.3
  • 8
    • 0000596922 scopus 로고
    • Intersystem crossing and internal conversion quantum yields of acridine in polar and nonpolar solvents
    • Kellmann, A. Intersystem crossing and internal conversion quantum yields of acridine in polar and nonpolar solvents. J. Phys. Chem. 81, 1195-1198 (1977).
    • (1977) J. Phys. Chem , vol.81 , pp. 1195-1198
    • Kellmann, A.1
  • 9
    • 0001675545 scopus 로고
    • Photophysical behavior of coumarins as a function of substitution and solvent: Experimental evidence for the existence of a lowest lying 1(n, p*) state
    • Seixas de Melo, J.S., Becker, R.S. & Macanita, A.L. Photophysical behavior of coumarins as a function of substitution and solvent: experimental evidence for the existence of a lowest lying 1(n, p*) state. J. Phys. Chem. 98, 6054-6058 (1994).
    • (1994) J. Phys. Chem , vol.98 , pp. 6054-6058
    • Seixas De Melo, J.S.1    Becker, R.S.2    Macanita, A.L.3
  • 10
    • 33846310399 scopus 로고    scopus 로고
    • Environmentsensitive fluorophore emitting in protic environments. Org
    • Uchiyama, S., Takehira, K., Yoshihara, T., Tobita, S. & Ohwada, T. Environmentsensitive fluorophore emitting in protic environments. Org. Lett. 8, 5869-5872 (2006).
    • (2006) Lett , vol.8 , pp. 5869-5872
    • Uchiyama, S.1    Takehira, K.2    Yoshihara, T.3    Tobita, S.4    Ohwada, T.5
  • 13
    • 0018786922 scopus 로고
    • Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene
    • Weber, G. & Farris, F.J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. Biochemistry 18, 3075-3078 (1979).
    • (1979) Biochemistry , vol.18 , pp. 3075-3078
    • Weber, G.1    Farris, F.J.2
  • 14
    • 0037204951 scopus 로고    scopus 로고
    • Probing protein electrostatics with a synthetic fluorescent amino acid
    • Cohen, B.E. et al. Probing protein electrostatics with a synthetic fluorescent amino acid. Science 296,1700-1703 (2002).
    • (2002) Science , vol.296 , pp. 1700-1703
    • Cohen, B.E.1
  • 15
    • 33644534146 scopus 로고    scopus 로고
    • Single-molecule visualization of environment-sensitive fluorophores inserted into cell membranes by staphylococcal gamma-hemolysin
    • Nguyen, A.H., Nguyen, V.T., Kamio, Y & Higuchi, H. Single-molecule visualization of environment-sensitive fluorophores inserted into cell membranes by staphylococcal gamma-hemolysin. Biochemistry 45, 2570-2576 (2006).
    • (2006) Biochemistry , vol.45 , pp. 2570-2576
    • Nguyen, A.H.1    Nguyen, V.T.2    Kamio, Y.3    Higuchi, H.4
  • 16
    • 20844456605 scopus 로고    scopus 로고
    • [Aladan3]TIPP: A fluorescent 5-opioid antagonist with high 5-receptor binding affinity and 5 selectivity
    • Chen, H. et al. [Aladan3]TIPP: a fluorescent 5-opioid antagonist with high 5-receptor binding affinity and 5 selectivity. Biopolymers 80, 325-331 (2005).
    • (2005) Biopolymers , vol.80 , pp. 325-331
    • Chen, H.1
  • 17
    • 78651058006 scopus 로고
    • Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin
    • Weber, G. Polarization of the fluorescence of macromolecules. II. Fluorescent conjugates of ovalbumin and bovine serum albumin. Biochem. J. 51, 155-167 (1952).
    • (1952) Biochem. J , vol.51 , pp. 155-167
    • Weber, G.1
  • 18
    • 24744463670 scopus 로고    scopus 로고
    • Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C
    • Turner, J.H. & Raymond, J.R. Interaction of calmodulin with the serotonin 5-hydroxytryptamine2A receptor. A putative regulator of G protein coupling and receptor phosphorylation by protein kinase C. J. Biol. Chem. 280, 30741-30750 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 30741-30750
    • Turner, J.H.1    Raymond, J.R.2
  • 20
    • 33745633570 scopus 로고    scopus 로고
    • Ageneticallyencodedfluorescentaminoacid
    • Summerer, D.etal. Ageneticallyencodedfluorescentaminoacid. Proc. Natl.Acad. Sci. USA 103, 9785-9789 (2006).
    • (2006) Proc. Natl.Acad. Sci. USA , vol.103 , pp. 9785-9789
    • Summerer, D.1
  • 21
    • 0036231647 scopus 로고    scopus 로고
    • Structuralsimilarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: Use ofsite-specific fluorescent probes of local environment
    • Backovic, M., Stratikos, E., Lawrence, D.A. & Gettins, P.G. Structuralsimilarity of the covalent complexes formed between the serpin plasminogen activator inhibitor-1 and the arginine-specific proteinases trypsin, LMW u-PA, HMW u-PA, and t-PA: use ofsite-specific fluorescent probes of local environment. Protein Sci. 11, 1182-1191 (2002).
    • (2002) Protein Sci , vol.11 , pp. 1182-1191
    • Backovic, M.1    Stratikos, E.2    Lawrence, D.A.3    Gettins, P.G.4
  • 22
    • 0038034094 scopus 로고    scopus 로고
    • Fluorescent peptide probes for high-throughput measurement of protein phosphatases
    • Noble, J.E., Ganju, P. & Cass, A.E. Fluorescent peptide probes for high-throughput measurement of protein phosphatases. Anal. Chem. 75, 2042-2047 (2003).
    • (2003) Anal. Chem , vol.75 , pp. 2042-2047
    • Noble, J.E.1    Ganju, P.2    Cass, A.E.3
  • 23
    • 1942541370 scopus 로고    scopus 로고
    • Novel real-time sensors to quantitatively assess in vivo inositol 1,4,5-trisphosphate production in intact cells
    • Sugimoto, K. et al. Novel real-time sensors to quantitatively assess in vivo inositol 1,4,5-trisphosphate production in intact cells. Chem. Biol. 11, 475-485 (2004).
    • (2004) Chem. Biol , vol.11 , pp. 475-485
    • Sugimoto, K.1
  • 24
    • 10644293891 scopus 로고    scopus 로고
    • Improving the sensitivity and dynamic range of reagentless fluorescent immunosensors by knowledge-based design
    • Renard, M. & Bedouelle, H. Improving the sensitivity and dynamic range of reagentless fluorescent immunosensors by knowledge-based design. Biochemistry 43, 15453-15462 (2004).
    • (2004) Biochemistry , vol.43 , pp. 15453-15462
    • Renard, M.1    Bedouelle, H.2
  • 25
    • 13944263892 scopus 로고    scopus 로고
    • Utilization of a nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2 domain-binding peptide mimetic
    • Shi, Z.D. etal. Utilization of a nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2 domain-binding peptide mimetic. Bioorg. Med. Chem. Lett. 15, 1385-1388 (2005).
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 1385-1388
    • Shi, Z.D.1
  • 26
    • 0001462978 scopus 로고    scopus 로고
    • 4-Aminophthalimide derivatives as environment-sensitive probes
    • Saroja, G., Soujanya, T., Ramachandram, B. & Samanta, A. 4-Aminophthalimide derivatives as environment-sensitive probes. J. Fluoresc. 8, 405-410 (1998).
    • (1998) J. Fluoresc , vol.8 , pp. 405-410
    • Saroja, G.1    Soujanya, T.2    Ramachandram, B.3    Samanta, A.4
  • 27
    • 33750951913 scopus 로고    scopus 로고
    • Origin of the strong effect of protic solvents on the emission spectra, quantum yield of fluorescence and fluorescence lifetime of 4-aminophthalimide. Role of hydrogen bonds in deactivation of S1-4-aminophthalimide
    • Krystkowiak, E., Dobek, K. & Maciejewski, A. Origin of the strong effect of protic solvents on the emission spectra, quantum yield of fluorescence and fluorescence lifetime of 4-aminophthalimide. Role of hydrogen bonds in deactivation of S1-4-aminophthalimide. J. Photoch. Photobio. A 184, 250-264 (2006).
    • (2006) J. Photoch. Photobio. A , vol.184 , pp. 250-264
    • Krystkowiak, E.1    Dobek, K.2    Maciejewski, A.3
  • 28
    • 13644266900 scopus 로고    scopus 로고
    • Photophysics and biological applications of the environment-sensitive fluorophore 6-N, N-dimethylamino-2, naphthalimide
    • Vazquez, M.E., Blanco, J.B. & Imperiali, B. Photophysics and biological applications of the environment-sensitive fluorophore 6-N, N-dimethylamino-2, naphthalimide. J. Am. Chem. Soc. 127, 1300-1306 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 1300-1306
    • Vazquez, M.E.1    Blanco, J.B.2    Imperiali, B.3
  • 29
    • 39149104346 scopus 로고    scopus 로고
    • Tools for investigating peptide-protein interactions: Synthesis of anhydride precursors of the environment-sensitive fluorophores DMAP and 6-DMN
    • Sainlos, M. & Imperiali, B. Tools for investigating peptide-protein interactions: synthesis of anhydride precursors of the environment-sensitive fluorophores DMAP and 6-DMN. Nat. Protoc. 2, 3219-3225 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 3219-3225
    • Sainlos, M.1    Imperiali, B.2
  • 30
    • 7444227388 scopus 로고    scopus 로고
    • New environment-sensitive fluorescent amino acid for Fmoc-based solid phase peptide synthesis
    • Eugenio Vazquez, M., Rothman, D.M. & Imperiali, B. A new environment-sensitive fluorescent amino acid for Fmoc-based solid phase peptide synthesis. Org. Biomol. Chem. 2, 1965-1966 (2004).
    • (2004) Org. Biomol. Chem , vol.2 , pp. 1965-1966
    • Eugenio Vazquez, M.1    Rothman, D.M.2    Imperiali, B.A.3
  • 31
    • 33947308721 scopus 로고    scopus 로고
    • Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells
    • Venkatraman, P. et al. Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells. Nat. Chem. Biol. 3, 222-228 (2007).
    • (2007) Nat. Chem. Biol , vol.3 , pp. 222-228
    • Venkatraman, P.1
  • 32
    • 33745135409 scopus 로고    scopus 로고
    • 6-N, N-Dimethylamino-2,3-naphthalimide: A new environment-sensitive fluorescent probe in 5- and m-selective opioid peptides
    • Vazquez, M.E. etal. 6-N, N-Dimethylamino-2,3-naphthalimide: a new environment-sensitive fluorescent probe in 5- and m-selective opioid peptides. J. Med. Chem. 49, 3653-3658 (2006).
    • (2006) J. Med. Chem. , vol.49 , pp. 3653-3658
    • Vazquez, M.E.1
  • 33
    • 0035788370 scopus 로고    scopus 로고
    • NMR trial models: Experiences with the colicin immunity protein Im7and the p85a C-terminalSH2-peptide complex
    • Pauptit, R.A. et al. NMR trial models: experiences with the colicin immunity protein Im7and the p85a C-terminalSH2-peptide complex. Acta Crystallogr. D 57, 1397-1404 (2001).
    • (2001) Acta Crystallogr , vol.57 , pp. 1397-1404
    • Pauptit, R.A.1
  • 34
    • 0037195067 scopus 로고    scopus 로고
    • Structure ofa regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide
    • Donaldson, L.W., Gish, G., Pawson, T., Kay, L.E. & Forman-Kay, J.D. Structure ofa regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide. Proc. Natl. Acad. Sci. USA 99,14053-14058 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14053-14058
    • Donaldson, L.W.1    Gish, G.2    Pawson, T.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 35
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng, M. & Sala, C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24, 1-29 (2001).
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 36
    • 33746861956 scopus 로고    scopus 로고
    • Comparative structuralanalysis ofthe Erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity
    • Appleton, B.A. etal. Comparative structuralanalysis ofthe Erbin PDZ domain and the first PDZ domain of ZO-1. Insights into determinants of PDZ domain specificity. J. Biol. Chem. 281, 22312-22320 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 22312-22320
    • Appleton, B.A.1
  • 37
    • 39149093047 scopus 로고    scopus 로고
    • Tools for investigating peptide-protein interactions: Peptide incorporation ofenvironment-sensitive fluorophores through SPPS-based 'building block approach
    • Sainlos, M. & Imperiali, B. Tools for investigating peptide-protein interactions: peptide incorporation ofenvironment-sensitive fluorophores through SPPS-based 'building block approach. Nat. Protoc. 2, 3210-3218 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 3210-3218
    • Sainlos, M.1    Imperiali, B.2
  • 38
    • 33645522678 scopus 로고    scopus 로고
    • Alternative to piperidine in Fmoc solid-phase synthesis
    • Hachmann, J. & Lebl, M. Alternative to piperidine in Fmoc solid-phase synthesis. J. Comb. Chem. 8, 149 (2006).
    • (2006) J. Comb. Chem , vol.8 , pp. 149
    • Hachmann, J.1    Lebl, M.2
  • 39
    • 0026151057 scopus 로고
    • DBU as an Na-deprotecting reagent for the fluorenylmethoxycarbonyl group in continuous flow solid-phase peptide synthesis
    • Wade, J.D., Bedford, J., Sheppard, R.C. & Tregear, G.W. DBU as an Na-deprotecting reagent for the fluorenylmethoxycarbonyl group in continuous flow solid-phase peptide synthesis. Pept Res. 4, 194-199 (1991).
    • (1991) Pept Res , vol.4 , pp. 194-199
    • Wade, J.D.1    Bedford, J.2    Sheppard, R.C.3    Tregear, G.W.4
  • 40
    • 0034802373 scopus 로고    scopus 로고
    • Improved preparation of amyloid-ß peptides using DBU as Na-Fmoc deprotection reagent
    • Tickler, A.K., Barrow, C.J. & Wade, J.D. Improved preparation of amyloid-ß peptides using DBU as Na-Fmoc deprotection reagent. J. Pept. Sci. 7, 488-494 (2001).
    • (2001) J. Pept. Sci , vol.7 , pp. 488-494
    • Tickler, A.K.1    Barrow, C.J.2    Wade, J.D.3
  • 41
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson, P.E., Muir, T.W., Clark-Lewis, I. & Kent, S.B. Synthesis of proteins by native chemical ligation. Science 266, 776-779 (1994).
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 42
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir, T.W. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249-289 (2003).
    • (2003) Annu. Rev. Biochem , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 43
    • 0017157455 scopus 로고
    • New micro-test for detection of incomplete coupling reactions in solid-phase peptide-synthesis using 2,4,6- trinitrobenzenesulphonic acid
    • Hancock, W.S. & Battersby, J.E. A New micro-test for detection of incomplete coupling reactions in solid-phase peptide-synthesis using 2,4,6- trinitrobenzenesulphonic acid. Anal. Biochem. 71, 260-264 (1976).
    • (1976) Anal. Biochem , vol.71 , pp. 260-264
    • Hancock, W.S.1    Battersby, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.