Encapsulation of pyrene within self-assembled peptide amphiphile nanofibers

Mustafa O. Guler; Randal C. Claussen; Samuel I. Stupp

doi:10.1039/b509246a

Encapsulation of pyrene within self-assembled peptide amphiphile nanofibers

Mustafa O. Guler, Randal C. Claussen, Samuel I. Stupp^*

^*Corresponding author for this work

Materials Science and Engineering

Research output: Contribution to journal › Article › peer-review

103 Scopus citations

Abstract

Certain peptide amphiphiles (PAs) in aqueous media are known to form high-aspect-ratio cylindrical nanofibers with hydrophobic cores. Using cholesterol or palmitic acid as the hydrophobe and the biological adhesion epitope RGDS as the hydrophilic segment, we studied the encapsulation of pyrene, a small hydrophobic molecule, within the cores of the self-assembling PA nanofibers. Circular dichroism (CD), transmission electron microscopy (TEM) and fluorescence were used to characterize formation of the supramolecular structures. Pyrene excimer formation observed by fluorescence demonstrated the encapsulation and aggregation of pyrene within the hydrophobic cores. In addition, peptide amphiphiles covalently functionalized with pyrene linked to the hydrophobic portion of the molecule exhibited excimer formation upon self-assembly into nanofibers. Interestingly excimer formation was not observed in similar molecules that formed spherical aggregates rather than cylindrical nanofibers.

Original language	English (US)
Pages (from-to)	4507-4512
Number of pages	6
Journal	Journal of Materials Chemistry
Volume	15
Issue number	42
DOIs	https://doi.org/10.1039/b509246a
State	Published - Nov 14 2005

ASJC Scopus subject areas

General Chemistry
Materials Chemistry

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abstract = "Certain peptide amphiphiles (PAs) in aqueous media are known to form high-aspect-ratio cylindrical nanofibers with hydrophobic cores. Using cholesterol or palmitic acid as the hydrophobe and the biological adhesion epitope RGDS as the hydrophilic segment, we studied the encapsulation of pyrene, a small hydrophobic molecule, within the cores of the self-assembling PA nanofibers. Circular dichroism (CD), transmission electron microscopy (TEM) and fluorescence were used to characterize formation of the supramolecular structures. Pyrene excimer formation observed by fluorescence demonstrated the encapsulation and aggregation of pyrene within the hydrophobic cores. In addition, peptide amphiphiles covalently functionalized with pyrene linked to the hydrophobic portion of the molecule exhibited excimer formation upon self-assembly into nanofibers. Interestingly excimer formation was not observed in similar molecules that formed spherical aggregates rather than cylindrical nanofibers.",

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AU - Claussen, Randal C.

AU - Stupp, Samuel I.

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N2 - Certain peptide amphiphiles (PAs) in aqueous media are known to form high-aspect-ratio cylindrical nanofibers with hydrophobic cores. Using cholesterol or palmitic acid as the hydrophobe and the biological adhesion epitope RGDS as the hydrophilic segment, we studied the encapsulation of pyrene, a small hydrophobic molecule, within the cores of the self-assembling PA nanofibers. Circular dichroism (CD), transmission electron microscopy (TEM) and fluorescence were used to characterize formation of the supramolecular structures. Pyrene excimer formation observed by fluorescence demonstrated the encapsulation and aggregation of pyrene within the hydrophobic cores. In addition, peptide amphiphiles covalently functionalized with pyrene linked to the hydrophobic portion of the molecule exhibited excimer formation upon self-assembly into nanofibers. Interestingly excimer formation was not observed in similar molecules that formed spherical aggregates rather than cylindrical nanofibers.

AB - Certain peptide amphiphiles (PAs) in aqueous media are known to form high-aspect-ratio cylindrical nanofibers with hydrophobic cores. Using cholesterol or palmitic acid as the hydrophobe and the biological adhesion epitope RGDS as the hydrophilic segment, we studied the encapsulation of pyrene, a small hydrophobic molecule, within the cores of the self-assembling PA nanofibers. Circular dichroism (CD), transmission electron microscopy (TEM) and fluorescence were used to characterize formation of the supramolecular structures. Pyrene excimer formation observed by fluorescence demonstrated the encapsulation and aggregation of pyrene within the hydrophobic cores. In addition, peptide amphiphiles covalently functionalized with pyrene linked to the hydrophobic portion of the molecule exhibited excimer formation upon self-assembly into nanofibers. Interestingly excimer formation was not observed in similar molecules that formed spherical aggregates rather than cylindrical nanofibers.

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Encapsulation of pyrene within self-assembled peptide amphiphile nanofibers

Abstract

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