Electronic and vibrational optical activity of several peptides related to neurohypophyseal hormones: Disulfide group conformation

Pazderková, Markéta; Bednářová, Lucie; Dlouhá, Helena; Flegel, Martin; Lebl, Michal; Hlaváček, Jan; Setnička, Vladimı́r; Urbanová, Marie; Hynie, S.; Klenerová, Věra; Baumruk, Vladimı́r; Maloň, Petr

doi:10.1002/bip.22105

Cited by 11 publications

(9 citation statements)

References 71 publications

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“…Transitions between these disulfide conformations occur independently of the main ring conformation. The positive torsion angle is favored by 78.2 to 21.8 % and is consistent with experimental evidence (see e.g., [49]). The simulation suggests that g/g′ transitions are more frequent for open ring conformations than for saddle.…”

Section: Disulfide Bridgesupporting

confidence: 81%

Conformation and dynamics of 8-Arg-vasopressin in solution

et al. 2014

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Arginine-vasopressin was subjected to a long (11 μs) molecular dynamics simulation in aqueous solution. Analysis of the results by DASH and principal components analyses revealed four main ring conformations that move essentially independently of the faster-moving tail region. Two of these conformations (labeled "saddle") feature well-defined β-turns in the ring and conserved transannular hydrogen bonds, whereas the other two ("open") feature neither. The conformations have been identified and defined and are all of sufficient stability to be considered candidates for biological conformations in their cognate receptors.

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Section: Disulfide Bridgesupporting

confidence: 81%

Conformation and dynamics of 8-Arg-vasopressin in solution

et al. 2014

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“…In Raman spectra, frequency of the S-S stretching mode reflects conformation of the C α -C β -S-S -C β -C α fragment and Raman signals in the C-S stretching region reflect conformation of the C-C α -C β -S and S -C β -C α -C fragments [39]. The ROA signals originating in S-S stretching vibrations seem to reflect chirality of the disulfide groups, as indicated by previous preliminary theoretical and experimental studies [42][43][44].…”

Section: Introductionmentioning

confidence: 80%

Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges

et al. 2020

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We report an investigation of the role of disulfide bridges in the 27-residue antimicrobial peptide lasiocepsin (I) containing two disulfide groups (Cys8–Cys25, Cys17–Cys27) and three its analogs lacking one (II, III) or both (IV) native disulfides. Selective alternate incorporation of one or both disulfide bridges influences symmetry, conformation and biological properties of these peptides as demonstrated in their chiroptical (particularly Raman) properties. The effect of modifying the disulfide bridge pattern on the peptide secondary structure is investigated in water and in the presence of 2,2,2-trifluoroethanol and sodium dodecyl sulphate. A combination of experimental electronic and vibrational chiroptical data shows that both disulfide groups are necessary for stabilizing lasiocepsin secondary structure. While the Cys8–Cys25 disulfide group is important for sustaining lasiocepsin tertiary structure and maintaining its biological activity, the Cys17–Cys27 disulfide bridge has a supporting function consisting in reducing peptide flexibility.

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“…on dialkyl disulfides permitted assignment of the three types of ν (S‐S) Raman markers located at ~500, ~520, and ~540 cm −1 , to the ggg , ggt , and tgt rotamers, respectively, defined along the ‐C‐S‐S‐C‐ moiety. Because of its extreme simplicity, this Raman‐based conformational rule has received a great attention, not only for analyzing the disulfide markers of simple model compounds but also in the structural analysis of disulfide linkages in peptides and proteins . Meanwhile, the increasing progress in quantum chemistry calculations could bring the proof of reliability for the aforementioned simple rule by means of the Hartree–Fock and density functional theory data obtained basically from diethyl disulfide (Scheme (c)).…”

Section: Introductionmentioning

confidence: 99%

Disulfide linkage Raman markers: a reconsideration attempt

Hernández

Pflüger

López-Tobar

et al. 2014

J Raman Spectroscopy

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During the last decades, Raman spectroscopy has been routinely used for probing the conformational features of disulfide linkages in peptides and proteins. However, the interpretation of disulfide Raman markers is currently performed by a simple rule derived from the earliest observations on dialkyl disulfides. More precisely, this rule consists of the following: (1) in analyzing the Raman bands in the 550–500 cm−1 region ascribed to disulfide bond stretch motion, namely, ν(S‐S), and (2) assigning the three types of Raman markers observed at ~500, ~520, and ~540 cm−1 to three families of rotamers defined along the three successive bonds of the ‐C‐S‐S‐C‐ moiety, referred to as ggg, ggt, and tgt. In this report, we attempt to show that an accurate analysis of disulfide vibrational features needs the use of the five torsion angles (χ1, χ2, χ3, χ2', and χ1') along the five successive bonds joining the two α‐carbon atoms in the cystine (Cys‐Cys) unit. The present work is inspired by the disulfide conformational investigations performed by a statistical scan of numerous protein crystal and nuclear magnetic resonance data, taking into account the handedness (right and left) of a disulfide bridge, its spatial shape (Staple, Hook, and Spiral), as well as the signs of the two extreme torsion angles χ1 and χ1'. It appears that the combined use of the old and recent conformational notations allows a more accurate structural and vibrational analysis of disulfide linkage. Copyright © 2014 John Wiley & Sons, Ltd.

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Electronic and vibrational optical activity of several peptides related to neurohypophyseal hormones: Disulfide group conformation

Cited by 11 publications

References 71 publications

Conformation and dynamics of 8-Arg-vasopressin in solution

Conformation and dynamics of 8-Arg-vasopressin in solution

Chiroptical Properties and Conformation of Four Lasiocepsin-Related Antimicrobial Peptides: Structural Role of Disulfide Bridges

Disulfide linkage Raman markers: a reconsideration attempt

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