Bioactive peptides: solid-state and solution conformation of cyclolinopeptide A

Blasio, Benedetto Di; Rossi, Filomena; Benedetti, Ettore; Pavone, Vincenzo; Pedone, Carlo; Temussi, Piero Andrea; Zanotti, G.; Tancredi, Teodorico

doi:10.1021/ja00207a015

Cited by 80 publications

(82 citation statements)

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“…Ilamicin b I , 69 cyclolinopeptide A, 70 and its analogues7' are examples of cyclo-epta-and cyclo-nona-peptides containing the type I-ac turned structure. They have with important biological functions: Ilamicin b l is an antibiotic, inhibiting the growth of mycobacteria, while cyclolinopeptide A shows cytoprotective properties against toxic agents, such as phaIloidine.…”

Section: Discussionmentioning

confidence: 99%

Discovering protein secondary structures: Classification and description of isolated α-turns

Pavone¹,

Gaeta²,

Lombardi³

et al. 1996

Biopolymers

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120

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Section: Discussionmentioning

confidence: 99%

Discovering protein secondary structures: Classification and description of isolated α-turns

Pavone¹,

Gaeta²,

Lombardi³

et al. 1996

Biopolymers

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120

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“…We obtained 100 mg (yield 4%) of pure cyclo(AibLeu-Pro-Phe-Phe), Rf = 0.28 in CHC13-CH30H (95 : 5 ) and 970 mg (yield 19%) of pure c(Aib-Leu-Pro-PhePhe),, Rf = 0.21 in CHC13-CH30H (95 : 5 ) .…”

Section: Experimental Synthesismentioning

confidence: 97%

“…NOES have been converted in interproton distances using the method of Esposito and Pastore; as reference, the cross peak has been chosen that connects the resonances of the two couple of aromatic protons, (2, 6) and (3,5 ) , of Phe', corresponding to an interproton distance of 2.474 A. Distances have been calculated from the NOESY spectra obtained with a mixing time of 350 ms, both at 300 and 230 K. The calculated correlation time of the molecule, in these conditions, is 0.59 ns at 300 K and 0.83 ns at 230 K.…”

Section: Nmr Analysismentioning

confidence: 99%

Solution and solid state structure of an aib-containing cyclodecapeptide inhibiting the cholate uptake in hepatocytes

et al. 1996

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The conformational analysis of synthetic cyclodecapeptide c(Pro‐Phe‐Phe‐Aib‐Leu)2 related to the cyclolinopeptide A, in the solid state and solution, has been carried out by x‐ray diffraction and nmr spectroscopy. The structure of the monoclinic form obtained from methanol [a = 11.351(5) Å, b = 27.455(2) Å, c = 12.716(8) Å, β = 99.65(3)°; space group P21; Z = 2] shows the presence of six intramolecular NH˙˙˙CO hydrogen bonds, with formation of four turns (three of type I and one of type III) and two C16 ring structures. All peptide units are trans. The solution structure, as found by nmr, indicates that, at room temperature, the peptide is conformationally homogeneous; the structure determined is perfectly symmetrical and topologically similar to that found in the solid state. The cyclodecapeptide exhibits similar biological activity to cyclolinopeptide A. © 1997 John Wiley & Sons, Inc. Biopoly 40: 465–478, 1996

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“…1 A peculiarity of CLA structure is the presence of cis-amide bond between proline residues. The determination of the x-ray structure and the NMR structural analysis of CLA, [2][3][4] gave the basis to study the biological, structural, and conformational properties of CLA analogues and related compounds. [5][6][7][8][9][10][11][12][13][14][15] In solution, at room temperature, CLA exhibits marked conformational mobility leading to the presence of a mixture of several conformers.…”

Section: Introductionmentioning

confidence: 99%

Tetrazole analogues of cyclolinopeptide A: Synthesis, conformation, and biology

et al. 2002

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Linear and cyclic analogues of cyclolinopeptide A (CLA) with two dipeptide segments (Val(5)-Pro(6) and Pro(6)-Pro(7)) replaced by their tetrazole derivatives were synthesized by the SPPS technique and cyclized using TBTU (O-(benzotriazol-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate) reagent. The conformational properties of the c(Leu(1)-Ile(2)-Ile(3)-Leu(4)-Val(5)-Pro(6)-psi[CN(4)]-Ala(7)-Phe(8)-Phe(9)) were investigated by NMR and computational techniques. The overall solution structure of this cyclic peptide resembles that observed for the CLA in the solid state. These studies of cyclic tetrazole CLA analogue confirm that the 1,5-disubstituted tetrazole ring functions as an effective, well-tolerated cis-amide bond mimic in solution. The peptides were examined for their immunosuppressive activity in the humoral response test. For cyclic analogues the immunosuppressive activity, at low doses, is equal in magnitude to the activity presented by cyclosporin A and native CLA. The conformational and biological data seem indicate that the Pro-Pro-Phe-Phe moiety and the preservation of the CLA backbone conformation are important for immunosuppressive activity.

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Bioactive peptides: solid-state and solution conformation of cyclolinopeptide A

Cited by 80 publications

References 1 publication

Discovering protein secondary structures: Classification and description of isolated α-turns

Discovering protein secondary structures: Classification and description of isolated α-turns

Solution and solid state structure of an aib-containing cyclodecapeptide inhibiting the cholate uptake in hepatocytes

Tetrazole analogues of cyclolinopeptide A: Synthesis, conformation, and biology

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