Conformations of cyclic peptides. III. Cyclopentaglycyltyrosyl and related compounds

Kopple, Kenneth D.; Ohnishi, Masayuki; Go, Anita

doi:10.1021/ja01043a040

Cited by 189 publications

(100 citation statements)

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“…However, the scarcity of 'H:-'Hf+, NOEs and the values of the intra-residue 'J(IHN-'Hm) coupling constants (in the range 6-8 Hz) (Wuthrich, 1986), as well as the size (>5 ppb/K) of the temperature coefficients, -dd('HN)/dT (Table 4, Fig. 4) (Kopple et al, 1969;Ohniaihi and Uny, 1969), for residues in those regions of epilancin K7 in which no @-methyl-)lanthionines are present, indicates that this is not the case for epilancin K7 in aqueous solution. In water, the only regions of epilancin K7 where defined conformations seem to occur are in the rings, as Fig.…”

Section: Sequence Determination ; the 'Hi3c-hmbc Approachmentioning

confidence: 99%

Sequence Analysis by NMR Spectroscopy of the Peptide Lantibiotic Epilancin K7 from Staphylococcus epidermidis K7

Kamp

Horstink

Hooven

et al. 1995

European Journal of Biochemistry

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The amino acid sequence of the novel lantibiotic epilancin K7 from Staphylococcus epidermidis K7 was determined by NMR spectroscopy. NMR spectroscopy was used because sequencing by conventional Edman degradation techniques was prohibited by internal sequence blocks owing to the presence of modified residues. Epilancin K7 consists of 31 residues, including two a,P-didehydroalanine (one-letter code U) and two a$-didehydrobutyrine (0) residues, one lanthionine (A-S-A), two p-methyllanthionines (A*-S-A), and six lysines. Epilancin K7 has a molecular mass of 3032 5 1.5 Da. The amino acid sequence of epilancin K7 was derived from both through-space dipolar proton-proton interactions and throughbond scalar proton-carbon interactions as detected by two-dimensional 'H-NOESY, 'H-ROESY and threedimensional 'H-TOCSY-NOESY, and by two-dimensional 'H,'T-heteronuclear multiple-bond correlation spectroscopy, respectively. The sequence is as follows : r s i rshs7 XAUVLKOUIKVAKKYAKGVA*LA* AGANIOGGK.The N-terminal residue X partly resembles an alanine but its exact nature is unclear. The organization of the sulfide-bridge-containing (P-methyl-)lanthionines was revealed by 'H-NMR and 'H,I3C-NMR spectroscopy. Epilancin K7 has a linear structure and a high positive net charge, and therefore is classified as a type-A lantibiotic. NMR analysis of a degraded though still active form of epilancin K7 showed that two N-terminal residues of epilancin K7 were missing, owing to decomposition at the a$-didehydro alanine at position 3 ; it was called the epilancin K7-(3-31)-peptide (peptide fragment of epilancin K7 consisting of positions 3 -31). The usefulness of three-dimensional 'H-TOCSY-NOESY, and two-dimensional 'H,'3C-heter~n~~lear multiple-bond correlation spectroscopy at natural abundance for the study of (modified) polypeptides is demonstrated.Keywords. Bacteriocin; HMBC spectroscopy; lanthionine; post-translational modification; primary structure.Lantibiotics are defined as gene-encoded, ribosomally synthesized antimicrobial polypeptides (19-34 residues, 1800-3500 Da) that contain unusual (P-methyl-)lanthionines and a$-didehydro residues as the result of post-translational modifications Jung and Sahl, 1991;Bierbaum and Sahl, 1993;Hansen, 1993 Abbreviations. A* or Abu,, 2-aminobutyrine or P-methylalanine moiety of /hnethyllanthionine ; Ala,, alanine moiety of lanthionine and P-methyllanthionine ; C', main-chain carbonyl (C =0) carbon ; COSY, correlated spectroscopy; 6, chemical shift; U or Dha, a,b-didehydroalanine ; 0 or Dhb, a$-didehydrobutyrine ; DQ-COSY, double-quantum

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Section: Sequence Determination ; the 'Hi3c-hmbc Approachmentioning

confidence: 99%

Sequence Analysis by NMR Spectroscopy of the Peptide Lantibiotic Epilancin K7 from Staphylococcus epidermidis K7

Kamp

Horstink

Hooven

et al. 1995

European Journal of Biochemistry

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“…Nevertheless, the conformational analysis involves several approximations: (1) the relationship between the dihedral angle 0 (NH-CaH) and the measured three-bond coupling constant 3JHNCH (8,9)-a spectral parameter most useful when considered in combination with potential energy maps (10,11); (2) temperature (12) and solvent (13,14) dependences of chemical shifts and proton exchange rates (15)(16)(17) of peptide hydrogens as related to their solvent-exposed or solvent-shielded state.…”

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confidence: 99%

Conformational Studies of Oxytocin, Lysine Vasopressin, Arginine Vasopressin, and Arginine Vasotocin by Carbon-13 Nuclear Magnetic Resonance Spectroscopy

Walter

Prasad

Deslauriers

et al. 1973

Proc. Natl. Acad. Sci. U.S.A.

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Oxytocin, arginine vasopressin, lysine vasopressin, arginine vasotocin, as well as their cyclic and acyclic analogs, were studied by carbon-13 nuclear magnetic resonance spectroscopy in deuterium oxide and deuterated dimethylsulfoxide. Fourier-transformed spectra were obtained at 25. 16 MHz. The resonances of all carbon atoms have been assigned in both solvent systems; this includes tentative assignments of the carbonyl carbons. The spectra of arginine vasopressin and lysine vasopressin are essentially identical when compared in D20 or dimethylsulfoxide, but they differ from those of oxytocin. The spectrum of arginine vasotocin in D20 is intermediate between those of oxytocin and the vasopressins. These spectral differences are not only due to variations in constituent amino acids but are also a reflection of conformational differences of oxytocin, arginine vasotocin, and the vasopressins. All hormones are sensitive to changes in hydrogen ion concentration in both solvents; this was not observed with deamino analogs, which lack the terminal amino group.Conformational analysis of data from proton nuclear magnetic resonance ('H NMR) spectroscopy has contributed significantly to elucidation of the preferred solution conformations of oxytocin (1, 2) and lysine vasopressin ([Lys8]VP) (3-7). Nevertheless, the conformational analysis involves several approximations: (1) the relationship between the dihedral angle 0 (NH-CaH) and the measured three-bond coupling constant 3JHNCH (8, 9)-a spectral parameter most useful when considered in combination with potential energy maps (10, 11); (2)

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“…The conformations of the cyclic hexapeptides indicated in Fig. 2 (conformations a' and b') have been determined by x-ray diffraction (12,13) and in solution (14)(15)(16)(17). Furthermore, ,8-turns have been defined in many naturally occurring polypeptides (18)(19)(20)(21).…”

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confidence: 99%

A Molecular Theory of Ion-Conducting Channels: A Field-Dependent Transition Between Conducting and Nonconducting Conformations

Urry

1972

Proc. Natl. Acad. Sci. U.S.A.

135

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Structural and conformational requirements for an electric field-dependent transition between conducting and nonconducting macromolecular systems are: two kinetically interconvertible and energetically similar conformations, one conducting and the other nonconducting, which have axes spanning the lipid layer of biological membranes, but which have different net dipole -moments along those axes. Two examples are described. A previously defined helix, the TLD-helix now termed the #63,3-helix, is proposed as the conducting species, and the linear peptide correlate of the cyclic hexapeptide conformation containing two ,8-turns and an inversion element of symmetry is proposed as a nonconducting species. The latter is termed an anti-882-spiral and contains little or no net dipole moment per turn, whereas the j363,3-helix contains a net dipole moment along the helix axis of about 0.5 Debye per dipeptide unit. A related conducting and nonconducting pair with large net dipole moments of opposite sigp, termed s'yn-i36-spiral and j0%,4-helix, are also described. The spiral conformations are stabilized in a lipid layer by intermolecular hydrogen bonds, leading to a linear association of transmembrane structures. A conformational transition in one member of the array could lead to destabilization of an adjacent member of the array. The conformational analysis uses a concept of cyclic conformationswith linear conformational correlates.The anti-3862-spiral and #63,3-helix are derivable from the conformations of the cyclic structure L(L-Gly)3] , whereas the syn-132-spiral and 862,4-helix may be derived from the cyclic structure E(L-L-Gly)2 .The conformational analysis leads to the expectation that N-formyl-(L-Ala-L-Ala-Gly), would form conducting channels.If there should exist two kinetically interchangeable conformations that could span the lipid layer of biological membranes, but that would have substantially different net dipole moments oriented in transmembrane manner, then the application of an electric field across the membrane could lead to the interconversion from one species to the other. If one conformation is a conducting species, for example, a channel, and the other is nonconducting, then a field-dependent channel could form. It is the purpose of this manuscript to explicate two pairs of such conformations.A conducting transmembrane. channel has been described (refs 1-3 and Hladky, S. B. & Haydon, D. A., personal communication) that exhibits ion selectivity and a high specific conductance and for which a conformation has been proposed (4-6) and supported by spectroscopic data (6, 7). The proposed conformation is given in Fig. 1 for the ?6LD-helix of gramicidin A. As will be discussed in greater detail below, the term 6 3,s-helix is a more descriptive one. The fundamental requirement for this conformation is a specific aminoacid sequence. For gramicidin A, the requirement is an alternating (L-D),, optical isomeric sequence of hydrophobic amino acids with a glycine residue replacing one of the Dresidues. Acco...

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Conformations of cyclic peptides. III. Cyclopentaglycyltyrosyl and related compounds

Cited by 189 publications

References 0 publications

Sequence Analysis by NMR Spectroscopy of the Peptide Lantibiotic Epilancin K7 from Staphylococcus epidermidis K7

Sequence Analysis by NMR Spectroscopy of the Peptide Lantibiotic Epilancin K7 from Staphylococcus epidermidis K7

Conformational Studies of Oxytocin, Lysine Vasopressin, Arginine Vasopressin, and Arginine Vasotocin by Carbon-13 Nuclear Magnetic Resonance Spectroscopy

A Molecular Theory of Ion-Conducting Channels: A Field-Dependent Transition Between Conducting and Nonconducting Conformations

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