Chiral N-substituted glycines can form stable helical conformations

Folding and Design

Volumn 2, Issue 6, 1997, Pages 369-375

  Armand, Philippe ^a   Kirshenbaum, Kent ^b   Falicov, Alexis ^c   Dunbrack Jr , Roland L ^c   Dill, Ken A ^a   Zuckermann, Ronald N ^d   Cohen, Fred E ^b  

^a NOVARTIS PHARMA AG   (Switzerland)

^b Departments of Biomedical Sciences

^c Department of Pharmaceutical Chemistry ^*

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Molecular modeling; N substituted glycines; Peptoids; Protein folding; Protein structure

Indexed keywords

DRUG DERIVATIVE; GLYCINE; OLIGOPEPTIDE; PEPTOID; SARCOSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; STEREOISOMERISM;

AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; GLYCINE; OLIGOPEPTIDES; PEPTOIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SARCOSINE; STEREOISOMERISM;

EID: 0031302812     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00051-5     Document Type: Article

References (17)

1. Simon, RJ., et al., & Bartlett, P.A. (1992). Peptoids: a modular approach to drug discovery. Proc. Natl Acad. Sci. USA 89, 9367-9371.
2. Zuckermann, R.N., et al., & Moos, W.H. (1994). Discovery of nanomolar ligands for 7-transmembrane G-protein-coupled receptors from a diverse N-(substituted)glycine peptoid library. J. Med. Chem. 37, 2678-2685.
3. Zuckermann, R.N., Kerr, J.M., Kent, S.B.H. & Moos, W.H. (1992). Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis. J. Am. Chem. Soc. 114, 10646-10647.
4. Kirshenbaum, K., et al., & Zuckermann, R.N. (1997). Sequencespecific polypeptoids: a diverse family of heteropolymers with stable secondary structure. Proc. Natl Acad. Sci. USA, in press.
5. Moehle, K. & Hofmann, H.-J. (1996). Peptides and peptoids - a quantum chemical structure comparison. Biopolymers 38, 781-790.
6. Ramachandran, G.N., Ramakrishnan, C. & Sasisekharan, V. (1963). Stereochemistry of polypeptide chain configurations. J. Mot. Biol. 7, 95-99.
7. Cornell, W.D., et al., & Kollman, P.A. (1995). A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117, 5179-5197.
8. Cramer, C.J., Hawkins, G.D., Lynch, G.C., Giesen, D.J., Truhlar, D.G. & Liotard, D.A. (1994). AMSOL-version 4.5. QCPE14, 55-57.
9. Wada, A. (1976). The α-helix as an electric macro-dipole. Adv. Biophys. 9, 1 -63.
10. Nicholson, H., Anderson, D.E., Dao-pin, S. & Matthews, B.W. (1991). Analysis of the interaction between charged side chains and the a-helix using designed thermostable mutants of phage T4 lysozyme. Biochemistry 30, 9816-9828.
11. as and protein stability. Biochemistry 31, 2253-2258.
12. Armstrong, K.M. & Baldwin, R.L (1993). Charged histidine affects αa-helix stability at all positions in the helix by interacting with the backbone charges. Proc. Natl Acad. Sci. USA 90, 11337-11340.
13. Creighton, T.E. (1993). Proteins: Structures and Molecular Properties. (2nd edn), W.H. Freeman, New York, USA.
14. Dill, K.A. (1990). Dominant forces in protein folding. Biochemistry 29, 7133-7155.
15. Press, W.H., Teukolsky, S.A., Vetterling, W.T. & Flannery, B.P. (1992). Numerical Recipes in C. Cambridge University Press, Cambridge, UK.
16. Kirkpatrick, S., Gelatt, C.D., Jr & Vecchi, M. (1983). Optimization by simulated annealing. Science 220, 671 -680.
17. 13C resonances of N-substituted glycine peptoids. J. Magn Reson.Ser. B 110, 195-197.