Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

Macquaire, François; Baleux, Françoise; Giaccobi, E; Huynh‐Dinh, Tam; Jm, Neumann; Sanson, Alain

doi:10.1021/bi00124a018

Cited by 38 publications

(22 citation statements)

References 34 publications

(37 reference statements)

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“…[17][18][19] Introduction of disulfide bridges can stabilize folded structures 20 by destabilizing unfolded ones. 32 A Fourier transform infrared reflection absorption spectroscopic study of N-octadecanoyl (Gly) n ethyl ester monolayers and Langmuir-Blodgett films, where n ϭ 1-5, demonstrated that the peptide-amphiphiles could form polyGly II helices while the oligoGly peptides themselves could not. Such noncovalent assemblies have utilized (a) chelators attached to peptides and appropriate metals to initiate interstrand association [21][22][23][24] or (b) lipids covalently attached to peptides that promote association via hydrophobic interactions.…”

Section: Introductionmentioning

confidence: 99%

Induction of protein‐like molecular architecture by monoalkyl hydrocarbon chains

Forns¹,

Lauer‐Fields²,

Gao³

et al. 2000

Biopolymers

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Numerous approaches have been described for creating relatively small folded biomolecular structures. "Peptide-amphiphiles," whereby monoalkyl or dialkyl hydrocarbon chains are covalently linked to peptide sequences, have been shown previously to form specific molecular architecture of enhanced stability. The present study has examined the use of monoalkyl hydrocarbon chains as a more general method for inducing protein-like structures. Peptide and peptide-amphiphiles have been characterized by CD and one- and two-dimensional nmr spectroscopic techniques. We have examined two structural elements: alpha-helices and collagen-like triple helices. The alpha-helical propensity of a 16-residue peptide either unmodified or acylated with a C(6) or C(16) monoalkyl hydrocarbon chain has been examined initially. The 16-residue peptide alone does not form a distinct structure in solution, whereas the 16-residue peptide adopts predominantly an alpha-helical structure in solution when a C(6) or C(16) monoalkyl hydrocarbon chain is N-terminally acylated. The thermal stability of the alpha-helix is greater upon addition of the C(16) compared with the C(6) chain, which correlates to the extent of aggregation induced by the respective hydrocarbon chains. Very similar results are seen using a 39-residue triple-helical model peptide, in that structural thermal stability (a) is increasingly enhanced as alkyl chain length is increased and (b) correlates to the extent of peptide-amphiphile aggregation. Overall, structures as diverse as alpha-helices, triple helices, and turns/loops have been shown to be induced and/or stabilized by alkyl chains. Increasing alkyl chain length enhances stability of the structural element and induces aggregates of defined sizes. Hydrocarbon chains may be useful as general tools for protein-like structure initiation and stabilization as well as biomaterial modification.

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Section: Introductionmentioning

confidence: 99%

Induction of protein‐like molecular architecture by monoalkyl hydrocarbon chains

Forns¹,

Lauer‐Fields²,

Gao³

et al. 2000

Biopolymers

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“…However, the effect of such an environment is exemplary. In a recent paper (Macquaire et al, 1992b), we showed that a membrane-like interface was able to induce a specific secondary structure in a small peptide anchored within the interface. In the present paper, we report the influence of the same micellar environment on a peptide the size of which is larger than that of lipidic molecules.…”

mentioning

confidence: 96%

Proton NMR conformational study of an annexin I fragment: Influence of a phospholipidic micellar environment

Macquaire

Baleux²,

Huynh‐Dinh³

et al. 1993

Biochemistry

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A 32 residue peptide, Ac-AQWDADELRAAMKGLGTDEDTLIELASRTNK, spanning the first helix-loop-helix motif of the second repeat of human annexin I, was synthesized and studied by standard 2D proton NMR and molecular modeling. The peptide was solubilized either in aqueous solution, in TFE-H2O mixtures or in aqueous phospholipidic micellar solution. In pure aqueous solution, elements of helix secondary structure were observed. Addition of TFE led to a dramatic cooperative effect on the secondary structure with a very low transition midpoint indicative of the strong tendency of the peptide to form alpha helices. Only in the aqueous micellar solution was the full helix-loop-helix motif obtained, showing again the potency of a membrane-like micellar environment to initiate peptide secondary structures and even elements of tertiary structure. There were sufficient NMR data to perform molecular modeling of the structure of the annexin fragment solubilized in the presence of micelles. However, this structure showed a relatively high degree of flexibility, especially around the T17-D18 hinge at the end of the loop.

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“…Moreover, liposomes as lipid carriers have been extensively evaluated as delivery vehicles for drugs, genes and/or cosmetics [12]. Liposomes undergo the problem of both chemical and physical instability; hence, the concept of proliposomes was introduced [13].…”

Section: Liposomes/niosomes and Their Pro-formsmentioning

confidence: 99%

Hydrogels and Their Combination with Liposomes, Niosomes, or Transfersomes for Dermal and Transdermal Drug Delivery

Ibrahim¹,

Nair²,

Al‐Dhubiab³

et al. 2017

Liposomes

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Polymeric networks that retain and absorb substantial amount of water or biological fluids and resemble as a biological tissue are defined as hydrogels. On the other hand, liposomes, transfersomes and niosomes are lipid carriers, which represent one of the major research and development focus areas of the pharmaceutical industry. They have great potential as lipid vehicles that are able to enhance permeation of drugs across the intact skin and can act as local depot for the drug to sustain and control its delivery. Lipid carrier and hydrogel combinations offer transdermal drug delivery of great potential to enhance systemic effects of both hydrophilic and lipophilic drugs. Also, lipid carriers can target drugs to skin appendages and improve transdermal delivery. Lipid carrier proform systems in the form of gelly liquid crystals can also be used transdermally for better drug absorption enhancement. This review highlights the potential of hydrogels and emulgels with or without lipid nanocarriers for dermal and transdermal application.

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Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

Cited by 38 publications

References 34 publications

Induction of protein‐like molecular architecture by monoalkyl hydrocarbon chains

Induction of protein‐like molecular architecture by monoalkyl hydrocarbon chains

Proton NMR conformational study of an annexin I fragment: Influence of a phospholipidic micellar environment

Hydrogels and Their Combination with Liposomes, Niosomes, or Transfersomes for Dermal and Transdermal Drug Delivery

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