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Volumn 65, Issue 1, 2005, Pages 113-129

Aromatic interactions in tryptophan-containing peptides: Crystal structures of model tryptophan peptides and phenylalanine analogs

Author keywords

Aromatic interactions; Crystal structures; Peptide conformations; Superhelical structure; Tryptophan peptides

Indexed keywords

ACETYLLEUCYLPHENYLALANYLVALINE O METHYL ESTER; ACETYLLEUCYLTRYPTOPHYLVALINE O METHYL ESTER; AROMATIC AMIDE; PEPTIDE; PHENYLALANINE DERIVATIVE; TERT BUTYLOXYCARBONYLALANYL ALPHA AMINO ISOBUTYRIC ACID LEUCYLTRYPTOPHYLVALINE O METHYL ESTER; TERT BUTYLOXYCARBONYLLEUCYLPHENYLALANYLVALINE O METHYL ESTER; TERT BUTYLOXYCARBONYLLEUCYLTRYPTOPHYLVALINE O METHYL ESTER; TRYPTOPHAN; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 14044256505     PISSN: 1397002X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3011.2004.00191.x     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 0022450133 scopus 로고
    • Aminoaromatic interactions in proteins
    • Burley, S.K. & Petsko, G.A. (1986) Aminoaromatic interactions in proteins. FEES Lett. 203, 139-143.
    • (1986) FEES Lett. , vol.203 , pp. 139-143
    • Burley, S.K.1    Petsko, G.A.2
  • 2
    • 0000347691 scopus 로고    scopus 로고
    • A gradient-corrected density functional study of indole self-association through N-H...π hydrogen bonding
    • Pejov, L. (2001) A gradient-corrected density functional study of indole self-association through N-H...π hydrogen bonding. Chem. Phys. Lett. 339, 269-278.
    • (2001) Chem. Phys. Lett. , vol.339 , pp. 269-278
    • Pejov, L.1
  • 3
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley, S.K. & Petsko, G.A. (1985) Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science 229, 23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 4
    • 0000192455 scopus 로고    scopus 로고
    • An ab initio and data mining study on aromatic-amide interactions
    • Duan, G., Smith, V.H. Jr & Weaver, D.F. (1999) An ab initio and data mining study on aromatic-amide interactions. Chem. Phys. Lett. 310, 323-332.
    • (1999) Chem. Phys. Lett. , vol.310 , pp. 323-332
    • Duan, G.1    Smith Jr., V.H.2    Weaver, D.F.3
  • 5
    • 0035965717 scopus 로고    scopus 로고
    • Investigation of aromatic-backbone amide interactions in the model peptide acetyl-Phe-Gly-Gly-N-methyl amide using molecular dynamics simulations and protein database search
    • Toth, G., Murphy, R.F. & Lovas, S. (2001) Investigation of aromatic-backbone amide interactions in the model peptide acetyl-Phe-Gly-Gly-N- methyl amide using molecular dynamics simulations and protein database search. J. Am. Chem. Soc. 123, 11782-11790.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11782-11790
    • Toth, G.1    Murphy, R.F.2    Lovas, S.3
  • 6
    • 0026557830 scopus 로고
    • The function of tryptophan residues in membrane proteins
    • Schiffer, M., Chang, C.-H. & Stevens, F.J. (1992) The function of tryptophan residues in membrane proteins. Protein Eng. 5, 213-214.
    • (1992) Protein Eng. , vol.5 , pp. 213-214
    • Schiffer, M.1    Chang, C.-H.2    Stevens, F.J.3
  • 7
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
    • Hu, W., Lee, K.-C. & Cross, T.A. (1993) Tryptophans in membrane proteins: indole ring orientations and functional implications in the gramicidin channel. Biochemistry 32, 7035-7047.
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.-C.2    Cross, T.A.3
  • 8
    • 0028787147 scopus 로고
    • Tryptophan hydrogen bonding and electric dipole moments: Functional roles in the gramicidin channel and implications for membrane proteins
    • Hu, W. & Cross, T.A. (1995) Tryptophan hydrogen bonding and electric dipole moments: functional roles in the gramicidin channel and implications for membrane proteins. Biochemistry 34, 14147-14155.
    • (1995) Biochemistry , vol.34 , pp. 14147-14155
    • Hu, W.1    Cross, T.A.2
  • 9
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.-M., Wimley, W.C., Gawrisch, K. & White, S.H. (1998) The preference of tryptophan for membrane interfaces. Biochemistry 37, 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 10
    • 0007461231 scopus 로고    scopus 로고
    • Indoles at interfaces: Calculations of electrostatic effects with density functional and molecular dynamics methods
    • Woolf, T.B., Grossfield, A. & Pearson, J.G. (1999) Indoles at interfaces: calculations of electrostatic effects with density functional and molecular dynamics methods. Int. J. Quantum Chem. 75, 197-206.
    • (1999) Int. J. Quantum Chem. , vol.75 , pp. 197-206
    • Woolf, T.B.1    Grossfield, A.2    Pearson, J.G.3
  • 11
    • 0036500833 scopus 로고    scopus 로고
    • Making a network of Hydrophobic clusters
    • Baldwin, R.L. (2002) Making a network of Hydrophobic clusters. Science 295, 165-166.
    • (2002) Science , vol.295 , pp. 165-166
    • Baldwin, R.L.1
  • 13
    • 0033179780 scopus 로고    scopus 로고
    • Packing of aromatic rings against tryptophan residues in proteins
    • Samanta, U., Pal, D. & Chakrabarti, P. (1999) Packing of aromatic rings against tryptophan residues in proteins. Acta Crystallogr. D55, 1421-1427.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1421-1427
    • Samanta, U.1    Pal, D.2    Chakrabarti, P.3
  • 18
    • 14044264841 scopus 로고    scopus 로고
    • Tryptophan-derived peptides: 1. Crystal structure and solution conformation of Boc-Gly-Trp-Ala-O'Bu
    • Anthoni, U., Christophersen, C., Flensburg, C., Jakobsen, M.H., Jensen, J. & Nielsen, P.H. (1996) Tryptophan-derived peptides: 1. Crystal structure and solution conformation of Boc-Gly-Trp-Ala-O'Bu. Struct. Chem. 7, 103-110.
    • (1996) Struct. Chem. , vol.7 , pp. 103-110
    • Anthoni, U.1    Christophersen, C.2    Flensburg, C.3    Jakobsen, M.H.4    Jensen, J.5    Nielsen, P.H.6
  • 20
    • 0033594361 scopus 로고    scopus 로고
    • Synthesis and dopamine receptor modulating activity of novel peptidomimetics of L-Prolyl-L-Leucyl-glycinamide featuring αα- disubstituted amino acids
    • Evans, M.C., Pradhan, A., Venkatraman, S., Ojala, W.H., Gleason, W.B., Mishra, R.K. & Johnson, R.L. (1999) Synthesis and dopamine receptor modulating activity of novel peptidomimetics of L-Prolyl-L-Leucyl-glycinamide featuring αα-disubstituted amino acids. J. Med. Chem. 42, 1441-1447.
    • (1999) J. Med. Chem. , vol.42 , pp. 1441-1447
    • Evans, M.C.1    Pradhan, A.2    Venkatraman, S.3    Ojala, W.H.4    Gleason, W.B.5    Mishra, R.K.6    Johnson, R.L.7
  • 21
    • 84977285614 scopus 로고
    • 5] enkephalin: Four cocrystallizing conformers with extended backbones that form an antiparallel β-sheet
    • 5] enkephalin: four cocrystallizing conformers with extended backbones that form an antiparallel β-sheet. Acta Crystallogr. B39, 625-637.
    • (1983) Acta Crystallogr. , vol.B39 , pp. 625-637
    • Karle, I.L.1    Karle, J.2
  • 22
    • 0018144087 scopus 로고
    • 5] enkephalin from X-ray diffraction: Features important for recognition at opiate receptor
    • 5] enkephalin from X-ray diffraction: features important for recognition at opiate receptor. Science 199, 1214-1216.
    • (1978) Science , vol.199 , pp. 1214-1216
    • Smith, G.D.1    Griffin, J.F.2
  • 24
    • 0021158372 scopus 로고
    • The stereochemistry of peptides containing alpha-aminoisobutyric acid
    • Prasad, B.V. V. & Balaram, P. (1984) The stereochemistry of peptides containing alpha-aminoisobutyric acid. CRC Crit. Rev. Biochem. 16, 307-348.
    • (1984) CRC Crit. Rev. Biochem. , vol.16 , pp. 307-348
    • Prasad, B.V.V.1    Balaram, P.2
  • 25
    • 0025345233 scopus 로고
    • Structural characteristics of α-helical peptide molecules containing Aib residues
    • Karle, I.L. & Balaram, P. (1990) Structural characteristics of α-helical peptide molecules containing Aib residues. Biochemistry 29, 6747-6756.
    • (1990) Biochemistry , vol.29 , pp. 6747-6756
    • Karle, I.L.1    Balaram, P.2
  • 26
    • 0036532444 scopus 로고    scopus 로고
    • First crystallographic signature of the highly ordered supramolecular helical assemblage from a tripeptide containing a non-coded amino acid
    • Halder, D., Maji, S.K., Sheldrick, W.S. & Banerjee, A. (2002) First crystallographic signature of the highly ordered supramolecular helical assemblage from a tripeptide containing a non-coded amino acid. Tetrahedron Lett. 43, 2653-2656.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 2653-2656
    • Halder, D.1    Maji, S.K.2    Sheldrick, W.S.3    Banerjee, A.4
  • 27
    • 0037194184 scopus 로고    scopus 로고
    • Self-assembly of a short peptide monomer into a continuous hydrogen bonded supramolecular helix: The crystallographic signature
    • Halder, D., Maji, S.K., Drew, M.G.B., Banerjee, A. & Banerjee, A. (2002) Self-assembly of a short peptide monomer into a continuous hydrogen bonded supramolecular helix: the crystallographic signature. Tetrahedron Lett. 43, 5465-5468.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 5465-5468
    • Halder, D.1    Maji, S.K.2    Drew, M.G.B.3    Banerjee, A.4    Banerjee, A.5
  • 28
    • 0037119781 scopus 로고    scopus 로고
    • Self-assembly of a tetrapeptide in which a unique supramolecular helical structure is formed via intermolecular hydrogen bonding in the solid state
    • Maji, S.K., Banerjee, A., Drew, M.G.B., Halder, D. & Banerjee, A. (2002) Self-assembly of a tetrapeptide in which a unique supramolecular helical structure is formed via intermolecular hydrogen bonding in the solid state. Tetrahedron Lett. 43, 6759-6762.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 6759-6762
    • Maji, S.K.1    Banerjee, A.2    Drew, M.G.B.3    Halder, D.4    Banerjee, A.5
  • 29
    • 0037102918 scopus 로고    scopus 로고
    • Structural analysis of peptide helices containing centrally positioned lactic acid
    • Aravinda, S., Shamala, N., Das, C. & Balaram, P. (2002) Structural analysis of peptide helices containing centrally positioned lactic acid. Biopolymers 64, 255-267.
    • (2002) Biopolymers , vol.64 , pp. 255-267
    • Aravinda, S.1    Shamala, N.2    Das, C.3    Balaram, P.4
  • 30
    • 11744374008 scopus 로고
    • Dimerization energetics of benzene and aromatic amino acid side chains
    • Burley, S.K. & Petsko, G.A. (1986) Dimerization energetics of benzene and aromatic amino acid side chains. J. Am. Chem. Soc. 108, 7995-8001.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7995-8001
    • Burley, S.K.1    Petsko, G.A.2
  • 32
    • 0038631832 scopus 로고    scopus 로고
    • Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing phenylalanine residues
    • Aravinda, S., Shamala, N., Das, C., Sriranjini, A., Karle, I.L. & Balaram, P. (2003) Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing phenylalanine residues. J. Am. Chem. Soc. 125, 5308-5315.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5308-5315
    • Aravinda, S.1    Shamala, N.2    Das, C.3    Sriranjini, A.4    Karle, I.L.5    Balaram, P.6
  • 33
    • 0037487158 scopus 로고    scopus 로고
    • Significance of aromatic-backbone amide interactions in protein structure
    • Toth, G., Watts, C.R., Murphy, R.F. & Lovas, S. (2001) Significance of aromatic-backbone amide interactions in protein structure. Proteins: Struct., Funct. Genet. 43, 373-381.
    • (2001) Proteins: Struct., Funct. Genet. , vol.43 , pp. 373-381
    • Toth, G.1    Watts, C.R.2    Murphy, R.F.3    Lovas, S.4
  • 34
    • 0034300761 scopus 로고    scopus 로고
    • A data mining and ab initio study of the interaction between the aromatic and backbone amide groups in proteins
    • Duan, G., Smith, V.H. Jr & Weaver, D.F. (2000) A data mining and ab initio study of the interaction between the aromatic and backbone amide groups in proteins. Int. J. Quantum Chem. 80, 44-60.
    • (2000) Int. J. Quantum Chem. , vol.80 , pp. 44-60
    • Duan, G.1    Smith Jr., V.H.2    Weaver, D.F.3
  • 35
    • 0034682341 scopus 로고    scopus 로고
    • Characterization of aromatic-amide (side-chain) interactions in proteins through systematic ab initio calculations and data mining analyses
    • Duan, G., Smith, V.H. Jr & Weaver, D.F. (2000) Characterization of aromatic-amide (side-chain) interactions in proteins through systematic ab initio calculations and data mining analyses. J. Phys. Chem. A 104, 4521-4532.
    • (2000) J. Phys. Chem. A , vol.104 , pp. 4521-4532
    • Duan, G.1    Smith Jr., V.H.2    Weaver, D.F.3
  • 37
    • 0038338832 scopus 로고    scopus 로고
    • Determination of chemical shielding tensor of an indole carbon and application to tryptophan orientation of a membrane peptide
    • Separovic, F., Ashida, J., Woolf, T., Smith, R. & Terao, T. (1999) Determination of chemical shielding tensor of an indole carbon and application to tryptophan orientation of a membrane peptide. Chem. Phys. Lett. 303, 493-498.
    • (1999) Chem. Phys. Lett. , vol.303 , pp. 493-498
    • Separovic, F.1    Ashida, J.2    Woolf, T.3    Smith, R.4    Terao, T.5
  • 38
    • 0000517116 scopus 로고    scopus 로고
    • Ab initio investigations on the photophysics of indole
    • Sobolewski, A. & Domcke, W. (1999) Ab initio investigations on the photophysics of indole. Chem. Phys. Lett. 315, 293-298.
    • (1999) Chem. Phys. Lett. , vol.315 , pp. 293-298
    • Sobolewski, A.1    Domcke, W.2
  • 39
    • 0037450579 scopus 로고    scopus 로고
    • Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone
    • Callis, P.R. & Vivian, J.T. (2003) Understanding the variable fluorescence quantum yield of tryptophan in proteins using QM-MM simulations. Quenching by charge transfer to the peptide backbone. Chem. Phys. Lett. 369, 409-414.
    • (2003) Chem. Phys. Lett. , vol.369 , pp. 409-414
    • Callis, P.R.1    Vivian, J.T.2
  • 40
    • 0345600243 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Trp side-chain conformational flexibility in the gramicidin A channel
    • Bingham, N.C., Smith, N.E.C., Cross, T.A. & Busath, D.D. (2003) Molecular dynamics simulations of Trp side-chain conformational flexibility in the gramicidin A channel. Biopolymers (Pept. Sci.) 71, 593-600.
    • (2003) Biopolymers (Pept. Sci.) , vol.71 , pp. 593-600
    • Bingham, N.C.1    Smith, N.E.C.2    Cross, T.A.3    Busath, D.D.4
  • 43
    • 84989457168 scopus 로고
    • Crystal structure and conformation of short linear peptides: Part VIII. L-leucyl-L-tryptophanyl-L-leucine hydrochloride dihydrate
    • Wu, S., Declercq, J.P., Tinant, B. & Meerssche, M.V. (1987) Crystal structure and conformation of short linear peptides: Part VIII. L-leucyl-L-tryptophanyl-L-leucine hydrochloride dihydrate. Bull. Soc. Chim. Belg. 96, 581-586.
    • (1987) Bull. Soc. Chim. Belg. , vol.96 , pp. 581-586
    • Wu, S.1    Declercq, J.P.2    Tinant, B.3    Meerssche, M.V.4
  • 45
  • 47
    • 37049079318 scopus 로고
    • Interaction of indole derivatives with biologically important aromatic compounds. Importance of simultaneous co-operation of hydrogen-bond pairing and stacking interactions for recognition of guanine base by a peptide: X-ray crystal analysis of 7-methylguanosine-5′-phosphate-tryptophanylglutamic acid complex
    • Ishida, T., Iyo, H., Ueda, H., Doi, M., Inoue, M., Nishimura, S. & Kitamura, K. (1991) Interaction of indole derivatives with biologically important aromatic compounds. Importance of simultaneous co-operation of hydrogen-bond pairing and stacking interactions for recognition of guanine base by a peptide: X-ray crystal analysis of 7-methylguanosine-5′-phosphate- tryptophanylglutamic acid complex. J. Chem. Soc. Perkin Trans, 1, 1847-1853.
    • (1991) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 1847-1853
    • Ishida, T.1    Iyo, H.2    Ueda, H.3    Doi, M.4    Inoue, M.5    Nishimura, S.6    Kitamura, K.7
  • 48
    • 0000714715 scopus 로고    scopus 로고
    • Aromatic van der Waals clusters: Structure and non-rigidity
    • Sun, S. & Bernstein, E.R. (1996) Aromatic van der Waals clusters: structure and non-rigidity. J. Phys. Chem. 100, 13348-13366.
    • (1996) J. Phys. Chem. , vol.100 , pp. 13348-13366
    • Sun, S.1    Bernstein, E.R.2
  • 49
    • 0032546782 scopus 로고    scopus 로고
    • π-stacking interactions alive and well in proteins
    • McGaughey, G.B., Gagnes, M. & Rappe, A.K. (1998) π-Stacking interactions alive and well in proteins. J. Biol. Chem. 273, 15458-15463.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagnes, M.2    Rappe, A.K.3
  • 50
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wuthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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