Double-helical cyclic peptides: Design, synthesis, and crystal structure of figure-eight mirror-image conformers of adamantane-constrained cystine- containing cyclic peptide cyclo (Adm-Cyst)3

Journal of Organic Chemistry

Volumn 65, Issue 14, 2000, Pages 4415-4422

  Ranganathan, Darshan ^a,c   Haridas, V ^a   Nagaraj, R ^b   Karle, Isabella L ^c  

^a INDIAN INSTITUTE OF CHEMICAL TECHNOLOGY   (India)

^b CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

^c NAVAL RESEARCH LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPEPTIDE;

ARTICLE; CRYSTAL STRUCTURE; FOURIER TRANSFORMATION; INFRARED SPECTROMETRY; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS; PROTON NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

CRYSTALLOGRAPHY, X-RAY; CYSTINE; DRUG DESIGN; MODELS, MOLECULAR; OLIGOPEPTIDES; PEPTIDES, CYCLIC; PROTEIN CONFORMATION;

EID: 0034647512     PISSN: 00223263     EISSN: None     Source Type: Journal    
DOI: 10.1021/jo0003807     Document Type: Article

References (33)

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21. The CD studies for all cyclopeptides reported in this paper were carried out in the wavelength region of 200-250 nm. The S-S chromophore of cystine unit is known to absorb at ∼260 nm (Woody, R. W.; Dunker, A. K. In Circular Dichroism and the Conformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1966; pp 109-157) and does not interfere in this region. The C=C chromophore of norbornene unit also does not absorb in this region as shown by us recently (J. Am. Chem. Soc. 1998, 120, 8448) in the comparison of olefinic and the dihydro analogues of norborneno peptides, wherein it was found that both exhibit a prominent positive CD band at ∼211 nm. A large number of cystine-containing cyclic peptides have been studied by us (Angew. Chem., Int. Ed. Engl. 1986, 35, 1105; J. Am. Chem. Soc. 1996, 118, 10916; J. Am. Chem. Soc. 1998, 120, 2695) for CD spectra and are found to absorb in the range of 210- 230 nm, the peptide chromophore region. We believe therefore that the CD bands exhibited by cystine-containing cyclic peptides described in the present work are largely due to normal peptide chromophores.
22. The CD studies for all cyclopeptides reported in this paper were carried out in the wavelength region of 200-250 nm. The S-S chromophore of cystine unit is known to absorb at ∼260 nm (Woody, R. W.; Dunker, A. K. In Circular Dichroism and the Conformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1966; pp 109-157) and does not interfere in this region. The C=C chromophore of norbornene unit also does not absorb in this region as shown by us recently (J. Am. Chem. Soc. 1998, 120, 8448) in the comparison of olefinic and the dihydro analogues of norborneno peptides, wherein it was found that both exhibit a prominent positive CD band at ∼211 nm. A large number of cystine-containing cyclic peptides have been studied by us (Angew. Chem., Int. Ed. Engl. 1986, 35, 1105; J. Am. Chem. Soc. 1996, 118, 10916; J. Am. Chem. Soc. 1998, 120, 2695) for CD spectra and are found to absorb in the range of 210- 230 nm, the peptide chromophore region. We believe therefore that the CD bands exhibited by cystine-containing cyclic peptides described in the present work are largely due to normal peptide chromophores.
23. The CD studies for all cyclopeptides reported in this paper were carried out in the wavelength region of 200-250 nm. The S-S chromophore of cystine unit is known to absorb at ∼260 nm (Woody, R. W.; Dunker, A. K. In Circular Dichroism and the Conformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1966; pp 109-157) and does not interfere in this region. The C=C chromophore of norbornene unit also does not absorb in this region as shown by us recently (J. Am. Chem. Soc. 1998, 120, 8448) in the comparison of olefinic and the dihydro analogues of norborneno peptides, wherein it was found that both exhibit a prominent positive CD band at ∼211 nm. A large number of cystine-containing cyclic peptides have been studied by us (Angew. Chem., Int. Ed. Engl. 1986, 35, 1105; J. Am. Chem. Soc. 1996, 118, 10916; J. Am. Chem. Soc. 1998, 120, 2695) for CD spectra and are found to absorb in the range of 210- 230 nm, the peptide chromophore region. We believe therefore that the CD bands exhibited by cystine-containing cyclic peptides described in the present work are largely due to normal peptide chromophores.
24. The CD studies for all cyclopeptides reported in this paper were carried out in the wavelength region of 200-250 nm. The S-S chromophore of cystine unit is known to absorb at ∼260 nm (Woody, R. W.; Dunker, A. K. In Circular Dichroism and the Conformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1966; pp 109-157) and does not interfere in this region. The C=C chromophore of norbornene unit also does not absorb in this region as shown by us recently (J. Am. Chem. Soc. 1998, 120, 8448) in the comparison of olefinic and the dihydro analogues of norborneno peptides, wherein it was found that both exhibit a prominent positive CD band at ∼211 nm. A large number of cystine-containing cyclic peptides have been studied by us (Angew. Chem., Int. Ed. Engl. 1986, 35, 1105; J. Am. Chem. Soc. 1996, 118, 10916; J. Am. Chem. Soc. 1998, 120, 2695) for CD spectra and are found to absorb in the range of 210- 230 nm, the peptide chromophore region. We believe therefore that the CD bands exhibited by cystine-containing cyclic peptides described in the present work are largely due to normal peptide chromophores.
25. The CD studies for all cyclopeptides reported in this paper were carried out in the wavelength region of 200-250 nm. The S-S chromophore of cystine unit is known to absorb at ∼260 nm (Woody, R. W.; Dunker, A. K. In Circular Dichroism and the Conformational Analysis of Biomolecules; Fasman, G. D., Ed.; Plenum Press: New York, 1966; pp 109-157) and does not interfere in this region. The C=C chromophore of norbornene unit also does not absorb in this region as shown by us recently (J. Am. Chem. Soc. 1998, 120, 8448) in the comparison of olefinic and the dihydro analogues of norborneno peptides, wherein it was found that both exhibit a prominent positive CD band at ∼211 nm. A large number of cystine-containing cyclic peptides have been studied by us (Angew. Chem., Int. Ed. Engl. 1986, 35, 1105; J. Am. Chem. Soc. 1996, 118, 10916; J. Am. Chem. Soc. 1998, 120, 2695) for CD spectra and are found to absorb in the range of 210-230 nm, the peptide chromophore region. We believe therefore that the CD bands exhibited by cystine-containing cyclic peptides described in the present work are largely due to normal peptide chromophores.
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