Cyclic peptides. 19. Cation binding of a cyclic dodecapeptide cyclo (L-Val-Gly-Gly-L-Pro)3 in an aprotic medium

Baron, D.; Lg, Pease; Er, Blout

doi:10.1021/ja00467a030

Cited by 33 publications

(14 citation statements)

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“…Another synthetic analogue of valinomycin, cyclo(L-Va1-Gly-Gly-~-Pro)~ [cycl~(VGGP)~l,' synthesized in our laboratory (Pease, 1975; Baron et a]., 1977), has been investigated using 'H and I3C N M R spectroscopy. In this compound Gly residues replace the two D residues of valinomycin, which may result in greater conformational freedom for the molecule.…”

Section: Cyclo(l-val-d-pro-d-val-l-pro)3mentioning

confidence: 99%

“…The decreased number of bulky side chains in this cyclic peptide relative to valinomycin and the earlier analogue may be expected to lead to greater access of complexed ions to solvent. An investigation of C J~~( V G G P )~, using circular dichroism (Baron et al, 1977), showed that this peptide forms stable complexes with alkali metal and alkaline earth metals and that the stabilities of the complexes are affected by both size and charges of the cations. It was shown that large cations (K', Ca*+, and Ba") form the most stable 1:l peptide-cation complexes and that of these the divalent ions bind more strongly by a large factor.…”

Section: Cyclo(l-val-d-pro-d-val-l-pro)3mentioning

confidence: 99%

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Cyclic peptides. 23. Conformations of an ion-binding cyclic peptide analog of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3

Easwaran¹,

Pease²,

Blout³

1979

Biochemistry

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A 270-MHz 1H nuclear magnetic resonance investigation of an ion-binding cyclic peptide analogue of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3, and its cation complexes is reported. In CD2Cl2 and CDCl3, the peptide is proposed to occur in a C3-symmetric conformer with the N--H's of all six glycine residues intramolecularly hydrogen bonded. This conformation is different from the familiar valinomycin bracelet structure and lacks any "cavity". Cations do not bind, or bind only weakly, to the peptide in these solvents. Uncomplexed cyclo(L-Val-Gly-Gly-L-Pro)3 in acetonitrile appears to be averaging among several conformations with no evidence found for any preferred intramolecular hydrogen bonds. The strong 1:1 complexes of cyclo(L-Val-Gly-Gly-L-Pro)3 with K+ ANd Ba2+ in acetonitrile are structurally analogous to the bracelet conformation of valinomycin and involve the N--H's of the Val residues and of the Gly's preceding Pro in intramolecular hydrogen bonding. Tl+ was also found to form strong 1:1 complexes with the dodecapeptide.

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Section: Cyclo(l-val-d-pro-d-val-l-pro)3mentioning

confidence: 99%

Section: Cyclo(l-val-d-pro-d-val-l-pro)3mentioning

confidence: 99%

Cyclic peptides. 23. Conformations of an ion-binding cyclic peptide analog of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3

Easwaran¹,

Pease²,

Blout³

1979

Biochemistry

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“…36) In the most extended circular form, the outside diameter of the space-filling model of valinomycin molecule is about 3.14 nm 2 •24) When the close-packing state of valinomycin is in a two-dimensional hexagonal lattice, the occupied area is estimated at 3.46 nm 2 . In Fig.…”

Section: Temperature-dependence Of Gramicidin A' and Valinomycin Monomentioning

confidence: 99%

Interaction of Phospholipid and Antibiotic Ionophores, GramicidinA′ and Valinomycin, in Mixed Monolayers

Mita¹,

Sairyo²

1992

Bioscience, Biotechnology, and Biochemistry

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“…7 Reagent grade perchlorates dried in vacuo at 120°C were used as alkali and alkaline earth metal salts. 2 Spectrometric grade acetonitrile (DOJINDO Laboratories) was used as the solvent for CD measurement without further purification. CD spectra were recorded on a Jasco J-500A automatic recording spectropolarimeter equipped with a DP-500 data processor.…”

Section: Experiments Almentioning

confidence: 99%

Macrocyclic Peptides VI. Complex Formations and Conformations of an Ionophorous Cyclic Octapeptide Containing N,N′-Ethylene-Bridged (S)-Leucyl-(S)-leucine and Glycine in Acetonitrile

Kojima

Ikeda

Iwadou

et al. 1991

Polym J

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ABSTRACT:Complex formations and conformations of a synthetic cyclic octapeptide, cyclo[Gly-ELL-Gly] 2 (1), with alkali and alkaline earth metal ions were investigated in acetonitrile by CD and NMR spectroscopies. The interactions between 1 and alkali metal complex ions (Li+, Na+, and K +) are considered to be very weak from small CD spectral changes. In the case of alkaline earth metal ions, titration curves obtained from CD data indicated the presence of only a PC (peptide-<:ation = I : I) complex ion for Mg 2 + and Ba 2 +, and of both P 2 C (peptide sandwich) and PC complex ions for Ca 2 +. The K 1 values evaluated from the titration curves were in the order of Ca 2+ > Ba 2+ > Mg 2 +. Furthermore, 1 H and 13 C NMR measurements showed that 1 and the complex ions with Ca2+ and Ba2+ have each different C 2-symmetric structure.KEY WORDS Solution Conformation / Cation-Binding Properties / CD Spectra/ Cyclic Octa peptide/ Glycine/ (S)-Leucine / 1 H and 13 C NMR / Piperazin-2-one / Ionophores form stable and lipophilic complexes with alkali and alkaline earth metal ions, and are able to transport them across membranes. It has been known that various cyclic peptides 1 ---4 and cyclic or acyclic polyether5 have an interesting feature to bind inorganic substrates such as alkali and alkaline earth metal ions, specifically. modes between organic substrates and cyclic peptides in comparison with those between inorganic substrates and cyclic peptides. Therefore, the authors have attempted to study the complex formation of a cyclic octapeptide (1) including ELL { L = (S)-leucine} with inorganic substrates.The authors have studied the interactions 6 between several novel cyclic peptides including N,N'-ethylene-bridged dipeptides {EXX; piperazin-2-one (MKP) derivatives} and organic substrates, and also found that these cyclic peptides are useful in the investigation 7 • 8 of the chiral recognition of (R)-and (S)-enatiomers. However, the conformations of organic substrate-cyclic peptide complexes have not been studied in detail because of the indefinite stoichiometries and the multiple coordination t To whom correspondence should be addressed. t , CH2-CH2

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Cyclic peptides. 19. Cation binding of a cyclic dodecapeptide cyclo (L-Val-Gly-Gly-L-Pro)3 in an aprotic medium

Cited by 33 publications

References 4 publications

Cyclic peptides. 23. Conformations of an ion-binding cyclic peptide analog of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3

Cyclic peptides. 23. Conformations of an ion-binding cyclic peptide analog of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3

Interaction of Phospholipid and Antibiotic Ionophores, GramicidinA′ and Valinomycin, in Mixed Monolayers

Macrocyclic Peptides VI. Complex Formations and Conformations of an Ionophorous Cyclic Octapeptide Containing N,N′-Ethylene-Bridged (S)-Leucyl-(S)-leucine and Glycine in Acetonitrile

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