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  1. Article: First series of

    Pypec, Maxime / Jouffret, Laurent / Taillefumier, Claude / Roy, Olivier

    Beilstein journal of organic chemistry

    2022  Volume 18, Page(s) 845–854

    Abstract: The synthesis and conformational analysis of the first series of peptoid oligomers composed of ... ...

    Abstract The synthesis and conformational analysis of the first series of peptoid oligomers composed of consecutive
    Language English
    Publishing date 2022-07-14
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2192461-2
    ISSN 1860-5397
    ISSN 1860-5397
    DOI 10.3762/bjoc.18.85
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Design of Triazolium-Grafted Peptidomimetic Macrocycles with Facial Amphipathicity to Target Pathogenic Bacteria.

    Guerinot, Cassandra / Malige, Mélodie / Charbonnel, Nicolas / Malosse, Killian / Jouffret, Laurent / Taillefumier, Claude / Roy, Olivier / Forestier, Christiane / Faure, Sophie

    Organic letters

    2024  Volume 26, Issue 19, Page(s) 4088–4092

    Abstract: Access to 1,2,3-triazolium-grafted peptoid macrocycles was developed by macrocyclization and multivalent postmodification of linear peptoid oligomers carrying an alternance of benzylic and propargyl groups as side chains. X-ray analysis and NMR studies ... ...

    Abstract Access to 1,2,3-triazolium-grafted peptoid macrocycles was developed by macrocyclization and multivalent postmodification of linear peptoid oligomers carrying an alternance of benzylic and propargyl groups as side chains. X-ray analysis and NMR studies revealed a conformational preference for constrained hairpin-shaped structures leading to the facial amphipathic character of these macrocycles. A preliminary evaluation showed the antimicrobial activities of these new cationic amphipathic architectures.
    MeSH term(s) Triazoles/chemistry ; Triazoles/pharmacology ; Molecular Structure ; Peptidomimetics/chemistry ; Peptidomimetics/pharmacology ; Peptidomimetics/chemical synthesis ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/chemical synthesis ; Microbial Sensitivity Tests ; Macrocyclic Compounds/chemistry ; Macrocyclic Compounds/pharmacology ; Macrocyclic Compounds/chemical synthesis ; Peptoids/chemistry ; Peptoids/pharmacology ; Peptoids/chemical synthesis ; Crystallography, X-Ray ; Bacteria/drug effects
    Language English
    Publishing date 2024-05-06
    Publishing country United States
    Document type Journal Article
    ISSN 1523-7052
    ISSN (online) 1523-7052
    DOI 10.1021/acs.orglett.4c01149
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Unveiling the conformational landscape of achiral all-

    Angelici, Gaetano / Bhattacharjee, Nicholus / Pypec, Maxime / Jouffret, Laurent / Didierjean, Claude / Jolibois, Franck / Perrin, Lionel / Roy, Olivier / Taillefumier, Claude

    Organic & biomolecular chemistry

    2022  Volume 20, Issue 40, Page(s) 7907–7915

    Abstract: The synthesis and conformational study ... ...

    Abstract The synthesis and conformational study of
    MeSH term(s) Peptoids/chemistry ; Protein Structure, Secondary ; Crystallography, X-Ray ; Models, Molecular ; Amides/chemistry
    Chemical Substances Peptoids ; Amides
    Language English
    Publishing date 2022-10-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2097583-1
    ISSN 1477-0539 ; 1477-0520
    ISSN (online) 1477-0539
    ISSN 1477-0520
    DOI 10.1039/d2ob01351g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Strengthening Peptoid Helicity through Sequence Site-Specific Positioning of Amide

    Rzeigui, Maha / Traikia, Mounir / Jouffret, Laurent / Kriznik, Alexandre / Khiari, Jameleddine / Roy, Olivier / Taillefumier, Claude

    The Journal of organic chemistry

    2020  Volume 85, Issue 4, Page(s) 2190–2201

    Abstract: The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence- ... ...

    Abstract The synthesis of biomimetic helical secondary structures is sought after for the construction of innovative nanomaterials and applications in medicinal chemistry such as the development of protein-protein interaction modulators. Peptoids, a sequence-defined family of oligomers, enable a peptidomimetic strategy, especially considering the easily accessible monomer diversity and peptoid helical folding propensity. However,
    Language English
    Publishing date 2020-01-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.9b02916
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4473: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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  5. Article ; Online: Multivalent thioglycopeptoids via photoclick chemistry: potent affinities towards LecA and BC2L-A lectins.

    Caumes, C / Gillon, E / Legeret, B / Taillefumier, C / Imberty, A / Faure, S

    Chemical communications (Cambridge, England)

    2015  Volume 51, Issue 61, Page(s) 12301–12304

    Abstract: Solution-phase synthesis of linear and cyclic β- and α,β-peptoids was coupled to photo-induced thiol-ene coupling reaction to readily access multivalent thioglycoclusters. A tetrameric cyclic β-peptoid scaffold displaying 1-thio-β-d-galactose or 1-thio-α- ...

    Abstract Solution-phase synthesis of linear and cyclic β- and α,β-peptoids was coupled to photo-induced thiol-ene coupling reaction to readily access multivalent thioglycoclusters. A tetrameric cyclic β-peptoid scaffold displaying 1-thio-β-d-galactose or 1-thio-α-d-mannose has revealed by ITC experiments efficient binding potency for bacterial lectins LecA and BC2L-A, respectively.
    MeSH term(s) Burkholderia cenocepacia/chemistry ; Click Chemistry ; Lectins/chemistry ; Molecular Structure ; Peptoids/chemical synthesis ; Peptoids/chemistry ; Photochemical Processes ; Pseudomonas aeruginosa/chemistry ; Sulfhydryl Compounds/chemical synthesis ; Sulfhydryl Compounds/chemistry
    Chemical Substances Lectins ; Peptoids ; Sulfhydryl Compounds
    Language English
    Publishing date 2015-08-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c5cc04646g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: NCα-gem-dimethylated peptoid side chains: A novel approach for structural control and peptide sequence mimetics.

    Shyam, Radhe / Nauton, Lionel / Angelici, Gaetano / Roy, Olivier / Taillefumier, Claude / Faure, Sophie

    Biopolymers

    2019  Volume 110, Issue 6, Page(s) e23273

    Abstract: The design of linear peptoid oligomers adopting well-defined secondary structures while mimicking defined peptide primary sequences is a major challenge in the context of drug discovery. To this end, chemists have developed cis-inducing peptoid side ... ...

    Abstract The design of linear peptoid oligomers adopting well-defined secondary structures while mimicking defined peptide primary sequences is a major challenge in the context of drug discovery. To this end, chemists have developed cis-inducing peptoid side chains to build robust polyproline type I helices. However, the number of efficient examples remains scarce and chemical diversity accessible through the use of these side chains is limited. Herein, we introduce an array of NCα-gem-dimethylated peptoid residues mimicking proteinogenic amino acids. Submonomer synthesis and block-coupling approaches were explored to access heterooligomers incorporating these novel types of side chains. NMR studies of monomer and trimer models showed that the NCα-gem-dimethylated groups exert complete cis control on the backbone amide conformation. Lastly, a preliminary molecular modeling study gave an insight into the preferred orientation of the substituents of the NCα-gem-dimethyl side chains relative to the peptoid backbone.
    MeSH term(s) Amines/chemistry ; Amino Acid Sequence ; Isomerism ; Methylation ; Molecular Dynamics Simulation ; Nuclear Magnetic Resonance, Biomolecular ; Peptides/chemistry ; Peptoids/chemistry ; Protein Structure, Secondary
    Chemical Substances Amines ; Peptides ; Peptoids
    Language English
    Publishing date 2019-03-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1123-x
    ISSN 1097-0282 ; 0006-3525
    ISSN (online) 1097-0282
    ISSN 0006-3525
    DOI 10.1002/bip.23273
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 77: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article ; Online: Antioxidant Activities of Peptoid-Grafted Chitosan Films.

    Elchinger, P-H / Delattre, C / Faure, S / Roy, O / Badel, S / Bernardi, T / Michaud, P / Taillefumier, C

    Applied biochemistry and biotechnology

    2017  Volume 181, Issue 1, Page(s) 283–293

    Abstract: The aim of this study was to investigate the possibility of immobilizing peptoid on chitosan film in order to generate new active material. Chitosan films have been grafted for the first time with short-length peptoid oligomers displaying antioxidant ... ...

    Abstract The aim of this study was to investigate the possibility of immobilizing peptoid on chitosan film in order to generate new active material. Chitosan films have been grafted for the first time with short-length peptoid oligomers displaying antioxidant activities. The antioxidant activity of the selected peptoids was initially investigated with the DPPH assay and hydroxyl radical procedure. The metal chelating capacity of peptoids was also evaluated prior to their covalent attachment to chitosan. The benefit of chitosan functionalization with respect to its intrinsic antioxidant properties was finally evaluated in the present study. Interestingly, an increase of up to 90 % of the antioxidant activity of chitosan was observed.
    MeSH term(s) Antioxidants/chemistry ; Antioxidants/pharmacology ; Biphenyl Compounds/chemistry ; Chitosan/chemistry ; Chitosan/pharmacology ; Food Packaging ; Humans ; Hydroxyl Radical/chemistry ; Oxidation-Reduction ; Oxidative Stress/drug effects ; Peptoids/chemistry ; Peptoids/pharmacology ; Picrates/chemistry
    Chemical Substances Antioxidants ; Biphenyl Compounds ; Peptoids ; Picrates ; Hydroxyl Radical (3352-57-6) ; Chitosan (9012-76-4) ; 1,1-diphenyl-2-picrylhydrazyl (DFD3H4VGDH)
    Language English
    Publishing date 2017-01
    Publishing country United States
    Document type Journal Article
    ZDB-ID 392344-7
    ISSN 1559-0291 ; 0273-2289
    ISSN (online) 1559-0291
    ISSN 0273-2289
    DOI 10.1007/s12010-016-2212-7
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 3053: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  8. Article ; Online: 1,2,3-Triazolium-Based Cationic Amphipathic Peptoid Oligomers Mimicking Antimicrobial Helical Peptides.

    Shyam, Radhe / Charbonnel, Nicolas / Job, Aurélie / Blavignac, Christelle / Forestier, Christiane / Taillefumier, Claude / Faure, Sophie

    ChemMedChem

    2018  Volume 13, Issue 15, Page(s) 1513–1516

    Abstract: Amphipathic cationic peptoids (N-substituted glycine oligomers) represent a promising class of antimicrobial peptide mimics. The aim of this study is to explore the potential of the triazolium group as a cationic moiety and helix inducer to develop ... ...

    Abstract Amphipathic cationic peptoids (N-substituted glycine oligomers) represent a promising class of antimicrobial peptide mimics. The aim of this study is to explore the potential of the triazolium group as a cationic moiety and helix inducer to develop potent antimicrobial helical peptoids. Herein we report the first solid-phase synthesis of peptoid oligomers incorporating 1,2,3-triazolium-type side chains and their evaluation against Escherichia coli, Enterococcus faecalis, and Staphylococcus aureus. Several triazolium-based oligomers, even of short length, selectively kill bacteria over mammalian cells. SEM visualization of S. aureus cells treated with a dodecamer and a hexamer reveals severe cell membrane damage and suggests that the longer oligomer acts by pore formation.
    MeSH term(s) Antimicrobial Cationic Peptides/chemistry ; Circular Dichroism ; Enterococcus faecalis/drug effects ; Escherichia coli/drug effects ; Microbial Sensitivity Tests ; Microscopy, Electron, Scanning ; Molecular Mimicry ; Peptoids/chemistry ; Polymers/chemistry ; Staphylococcus aureus/drug effects ; Triazoles/chemistry ; Triazoles/pharmacology
    Chemical Substances Antimicrobial Cationic Peptides ; Peptoids ; Polymers ; Triazoles
    Language English
    Publishing date 2018-07-04
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2218496-X
    ISSN 1860-7187 ; 1860-7179
    ISSN (online) 1860-7187
    ISSN 1860-7179
    DOI 10.1002/cmdc.201800273
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6280: Show issues Location:
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  9. Article ; Online: Weak backbone CH···O=C and side chain tBu···tBu London interactions help promote helix folding of achiral NtBu peptoids.

    Angelici, G / Bhattacharjee, N / Roy, O / Faure, S / Didierjean, C / Jouffret, L / Jolibois, F / Perrin, L / Taillefumier, C

    Chemical communications (Cambridge, England)

    2016  Volume 52, Issue 24, Page(s) 4573–4576

    Abstract: The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. ... ...

    Abstract The synthesis of all-cis amide (NtBu)-glycine oligomers up to 15 residues long by a blockwise coupling approach is reported. The structure and dynamical behavior of these peptoids have been studied by X-ray crystallography, NMR and molecular modeling. Analyses reveal that the folding of these oligomers is driven by weak CH···O=C hydrogen bonding along the peptoid backbone and London interaction between tBu···tBu side-chains.
    MeSH term(s) Crystallography, X-Ray ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Peptides/chemistry ; Protein Folding ; Proton Magnetic Resonance Spectroscopy ; Stereoisomerism
    Chemical Substances Peptides
    Language English
    Publishing date 2016-03-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c6cc00375c
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  10. Article ; Online: Correction: Weak backbone CHO[double bond, length as m-dash]C and side chain tButBu London interactions help promote helix folding of achiral NtBu peptoids.

    Angelici, G / Bhattacharjee, N / Roy, O / Faure, S / Didierjean, C / Jouffret, L / Jolibois, F / Perrin, L / Taillefumier, C

    Chemical communications (Cambridge, England)

    2016  Volume 52, Issue 39, Page(s) 6625

    Abstract: Correction for 'Weak backbone CHO[double bond, length as m-dash]C and side chain tButBu London interactions help promote helix folding of achiral NtBu peptoids' by G. Angelici et al., Chem. Commun., 2016, 52, 4573-4576. ...

    Abstract Correction for 'Weak backbone CHO[double bond, length as m-dash]C and side chain tButBu London interactions help promote helix folding of achiral NtBu peptoids' by G. Angelici et al., Chem. Commun., 2016, 52, 4573-4576.
    Language English
    Publishing date 2016-05-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c6cc90163h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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