Comprehensive determination of the cyclic FEE peptide chemical stability in solution

Bernard, Mélisande; Henriet, Théo; Fourgeaud, Martine; Fabreguettes, Jean-Roch; Surget, Estelle; Guyon, F.; Do, Bernard

doi:10.1016/j.jpba.2013.10.026

Cited by 6 publications

(4 citation statements)

References 16 publications

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Section: Resultssupporting

confidence: 71%

“…This represents conventionally the instrumental performance. The present data with previous ones 24 and the resolution provided by the MS instrument allowed elucidating the isotopic distribution of cFEE, being in complete correlation with its cyclic structure. Concomitantly, during the analysis, fragmentation by collision-induced dissociation (CID) was performed to investigate more precisely the structure of the compound.…”

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confidence: 71%

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Disorder-to-Order Markers of a Cyclic Hexapeptide Inspired from the Binding Site of Fertilin β Involved in Fertilization Process

et al. 2019

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Synthetic peptides mimicking the binding site of fertilin β to its receptor, integrin α6β1, were shown to inhibit sperm–egg fusion when added to in vitro media. In contrast, the synthetic cyclic hexapeptide, cyclo(Cys1-Ser2-Phe3-Glu4-Glu5-Cys6), named as cFEE, proved to stimulate gamete fusion. Owing to its biological specificity, this hexapeptide could help improve the in vitro fertilization pregnancy rate in human. In an attempt to establish the structure–activity relationship of cFEE, its structural dynamics was herein analyzed by means of ultraviolet circular dichroism (UV-CD) and Raman scattering. The low concentration CD profile in water, containing mainly a deep minimum at ∼202 nm, is consistent with a rather unordered chain. However, an ordering trend of the peptide loop has been observed in a less polar solvent such as methanol, where the UV-CD signal shape is formed by a double negative marker at ∼202/215 nm, indicating the presence of a type-II′ β-turn. Raman spectra recorded in aqueous samples upon a 100-fold concentration increase, still showed an important population (∼30%) of the disordered structure. The structural flexibility of the disulfide bridge was confirmed by the Raman markers arising from the Cys1-Cys6 disulfide bond-stretch motions. Density functional theory calculations highlighted the formation of the type-II′ β-turn on the four central residues of cFEE (i.e., -Ser2-Phe3-Glu4-Glu5-) either with a left- or with a right-handed disulfide. The structure with a left-handed S–S bond, however, appears to be more stable.

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Section: Resultssupporting

confidence: 71%

supporting

confidence: 71%

Disorder-to-Order Markers of a Cyclic Hexapeptide Inspired from the Binding Site of Fertilin β Involved in Fertilization Process

et al. 2019

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“…Usually, peptides with L-amino acids are susceptible to enzymatic degradation in circulation [30]. Even cyclic peptides can undergo degradation in vivo under certain conditions, depending on the sequence of amino acids in the peptide [31, 32]. The peptidomimetics were synthesized with the objective of inhibiting the HER2-based signaling pathway while improving enzymatic resistance by introducing the D-amino acids into the parent compound 18 .…”

Section: Resultsmentioning

confidence: 99%

Design of cyclic and d‐amino acids containing peptidomimetics for inhibition of protein‐protein interactions of HER2‐HER3

Pallerla

Naik

Singh

et al. 2018

Journal of Peptide Science

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HER2 receptors are surface proteins belonging to the epidermal growth factor family of receptors. Their numbers are elevated in breast, lung, and ovarian cancers. HER2-positive cancers are aggressive, have higher mortality rate, and have a poor prognosis. We have designed peptidomimetics that bind to HER2 and block the HER2-mediated dimerization of epidermal growth factor family of receptors. Among these, a symmetrical cyclic peptidomimetic (compound 18) exhibited antiproliferative activity in HER2-overexpressing lung cancer cell lines with IC values in the nanomolar concentration range. To improve the stability of the peptidomimetic, d-amino acids were introduced into the peptidomimetic, and several analogs of compound 18 were designed. Among the analogs of compound 18, compound 32, a cyclic, d-amino acid-containing peptidomimetic, was found to have an IC value in the nanomolar range in HER2-overexpressing cancer cell lines. The antiproliferative activity of compound 32 was also measured by using a 3D cell culture model that mimics the in vivo conditions. The binding of compound 32 to the HER2 protein was studied by surface plasmon resonance. In vitro stability studies indicated that compound 32 was stable in serum for 48 hours and intact peptide was detectable in vivo for 12 hours. Results from our studies indicated that 1 of the d-amino acid analogs of 18, compound 32, binds to the HER2 extracellular domain, inhibiting the phosphorylation of kinase of HER2.

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“…Lyophilized peptide was resuspended and aliquoted at 10 mM in human Continuous Single Culture Medium Complete (CSCM-C) (Fujifilm Irvine Scientific, Asni ere sur Seine, 90165, France). The detailed peptide sequence of human peptide is H-C(S-)-SFEE-C(S-)-OH (18). Human fluorescent cyclic fertilin (HiLyte Fluor 488-cFEE) was synthetized by Eurogentec (France).…”

Section: Peptide Synthesismentioning

confidence: 99%

Cyclic fertilin-derived peptide stimulates in vitro human embryo development

et al. 2022

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Comprehensive determination of the cyclic FEE peptide chemical stability in solution

Cited by 6 publications

References 16 publications

Disorder-to-Order Markers of a Cyclic Hexapeptide Inspired from the Binding Site of Fertilin β Involved in Fertilization Process

Disorder-to-Order Markers of a Cyclic Hexapeptide Inspired from the Binding Site of Fertilin β Involved in Fertilization Process

Design of cyclic and d‐amino acids containing peptidomimetics for inhibition of protein‐protein interactions of HER2‐HER3

Cyclic fertilin-derived peptide stimulates in vitro human embryo development

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