NMR studies on Ni(II) induced cyclization of a histidine-tagged peptide

Journal of Peptide Science

Volumn 8, Issue 11, 2002, Pages 634-641

  Spiga, Ottavia ^a   Bernini, Andrea ^a   Scarselli, Maria ^a   Ciutti, Arianna ^a   Giovannoni, Leonardo ^a   Laschi, Franco ^a   Bracci, Luisa ^a   Niccolai, Neri ^a  

^a UNIVERSITY OF SIENA   (Italy)

Author keywords

Nickel complex; NMR; Peptide folding; Peptide metal complex; Solution structure

Indexed keywords

HISTIDINE; NICKEL; PEPTIDE DERIVATIVE; CYCLOPEPTIDE; HYBRID PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHELATION; CONTROLLED STUDY; COVALENT BOND; CYCLIZATION; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CYCLIZATION; HISTIDINE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; NICKEL; PEPTIDES, CYCLIC; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT FUSION PROTEINS;

EID: 0036854568     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/psc.424     Document Type: Article

References (23)

1. Unden A, Bartfai T. Peptides as active probes. EXS Rev. 1995; 73: 229-255.
2. Borgia JA, Fields GB. Chemical synthesis of proteins. TIBTECH 2000; 18: 243-251.
3. Keire DA, Solomon TE, Reeve JR. Identical primary sequence but different conformations of the bioactive regions of canine CCK-8 and CCK-58. Biochem. Biophys. Res. Commun. 1999: 266: 400-404.
4. Ortiz TC, Devereaux MC, Parker KK. Structural variants of a human 5-HT1a receptor intracellular loop 3 peptide. Pharmacology 2000; 60: 195-202.
5. Di Maro D, Scarselli M, Bernini A, Cresti S, Rossolini GM, Lozzi L, Neri P, Niccolai N. On the structural stability of a small bioactive peptide of potential use in biotechnology. J. Biomol. Struct. Dyn. 1999; 16: 1053-1059.
6. Monnet C, Laune D, Laroche-Traineau J, Biard-Piechaczyk M, Briant L, Bes C, Pugniere M, Mani JC, Pau B, Cerutti M, Devauchelle G, Devaux C, Granier C, Chardes T. Synthetic peptides derived from the variable regions of an anti-CD4 monoclonal antibody bind to CD4 and inhibit HIV-1 promoter activation in virus-infected cells. J. Biol. Chem. 1999; 274: 3789-3796.
7. Fairlie DP, West ML, Wong AK. Towards protein surface mimetics. Curr. Med. Chem. 1998; 5: 29-62.
8. De Grado WF. Design of peptides and proteins. Adv. Protein Chem. 1988; 39: 51-124.
9. Ueda J, Ozawa T, Miyazaki M, Fujiwara Y. SOD-like activity of complexes of nickel(II) ion with some biologically important peptides and their novel reactions with hydrogen peroxide. Inorg. Chim. Acta 1993; 214: 29-32.
10. Ragsdale SW. Nickel biochemistry. Curr. Opin. Chem. Biol. 1998; 2: 208-215.
11. Spiga O, Scarselli M, Bernini A, Ciutti A, Giovannoni L, Laschi F, Bracci L, Niccolai N. Metal ion complexation and folding of linear peptides. Biophys. Chem. 2002; 97: 79-86.
12. Bal W, Jerzowka-Bojczuk M, Kasprzak KS. Binding of nickel(II) and copper(II) to the N-terminal sequence of human protamine HP2. Chem. Res. Toxicol. 1997; 10: 906-914.
13. Gasmi G, Singer A, Forman-Kay J, Sarkar B. NMR structure of neuromedin C, a neurotransmitter with an amino terminal CuII-, NiII-binding (ATCUN) motif. J. Peptide Res. 1997; 49: 500-509.
14. Zoroddu MA, Kowalik-Jankowska T, Kozlowsky H, Molinari H, Salnikov K, Broday L, Costa M. Interaction of Ni(II) and Cu(II) with a metal binding sequence of histone H4: AKRHRK, a model of the H4 tail. Biochim. Biophys. Acta 2000; 1475: 163-168.
15. König W, Geiger R. A new method for the synthesis of peptides: activation of the carboxy group with dicyclohexylcarbodiimide and the addition of 1-hydroxybenzotriazoles. Chem. Ber. 1970; 103: 788-798.
16. Balacco G. SwaN-MR: A complete and expansible NMR software for the MacIntosh. J. Chem. Inf. Comput. Sci. 1994; 34: 1235-1241.
17. Guntert P, Mumenthaler C, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 1997; 273: 283-298.
18. Cornell WD, Cieplak P, Bayly CI, Gould IR, Merz KM, Ferguson DM, Spellmeyer DC, Fox T, Caldwell JW, Kollman PA. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995; 117: 5179-5197.
19. Koradi R, Billeter M, Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 1996; 14: 51-55.
20. http://www.sdsc.edu/ResTools/biotools/biotools9. html
21. Bairoch A, Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 2000; 28: 45-48.
22. Zoroddu MA, Kowalik-Jankowska T, Kozlowski H, Salnikov K, Costa MJ. Ni(II) and Cu(II) binding with a 14-aminoacid sequence of Cap43 protein, TRSRSHT-SEGTRSR. J. Inorg. Biochem. 2001; 84: 47-54.
23. Némethy G, Printz MP. The γ-turn, a possible folded conformation of the polypeptide chain. Comparison with the β-turn. Macromolecules 1972: 5: 755-758.