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Self-assembly of recombinant amphiphilic oligopeptides into vesicles.

Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Research Abstract Details 

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  • Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Abstract Text:

    albert j van hellAlbert J van Hell,cristina i c a costaCristina I C A Costa,frits m fleschFrits M Flesch,marc sutterMarc Sutter,wim jiskootWim Jiskoot,daan j a crommelinDaan J A Crommelin,wim e henninkWim E Hennink,enrico mastrobattistaEnrico Mastrobattista,

    The aim of the present study was to design amphiphilic oligopeptides that can self-assemble into vesicular structures. The ratio of hydrophilic to hydrophobic block length was varied, and peptides were designed to have a hydrophobic tail in which the bulkiness of the amino acid side groups increases toward the hydrophilic domain (Ac-Ala-Ala-Val-Val-Leu-Leu-Leu-Trp-Glu(2/7)-COOH). These peptides were recombinantly produced in bacteria as an alternative to solid-phase synthesis. We demonstrate with different complementary techniques (dynamic and static light scattering, tryptophan fluorescence anisotropy, and electron microscopy) that these amphiphilic peptides spontaneously form vesicles with a radius of approximately 60 nm and a low polydispersity when dispersed in aqueous solution at neutral pH. Morphology and size of the vesicles were relatively insensitive to the variations in hydrophilic block length. Exposure to acidic pH resulted in formation of visible aggregates, which could be fully reversed to vesicles upon pH neutralization. In addition, it was demonstrated that water-soluble molecules can be entrapped inside these peptide vesicles. Such peptide vesicles may find applications as biodegradable drug delivery systems with a pH-dependent release profile.

    Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Publishing Authors By Initials

    aj van hellAJ van Hell,ci costaCI Costa,fm fleschFM Flesch,m sutterM Sutter,w jiskootW Jiskoot,dj crommelinDJ Crommelin,we henninkWE Hennink,e mastrobattistaE Mastrobattista,

    For similar chemical actions and uses: specialty uses of chemicals: surface-active agents research abstracts see: chemical actions and uses: specialty uses of chemicals: surface-active agents research

    PUBMED ID PMID:

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    Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Biomacromolecules

    VOLUME: 8

    Page Numbers: 2753-61

    Journal Abbreviation: Biomacromolecules

    ISSN: 1525-7797

    DAY: 14

    MONTH: 08

    YEAR: 2007

    Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 100892849

    Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Keywords Mesh Terms:

    KEYWORDS: Surface-Active Agents

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Self-assembly of recombinant amphiphilic oligopeptides into vesicles. Information

    Substance Name: fluorexon

    Registry Number: 1461-15-0

    Grant and Affiliation Information for Self-assembly of recombinant amphiphilic oligopeptides into vesicles.

    AFFILIATION: Department of Pharmaceutics, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Biomacromolecules

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