Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels

John B. Matson, Christina J. Newcomb, Ronit Bitton, Samuel I Stupp

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

High aspect ratio peptide nanofibers have potential as biodegradable vehicles for drug delivery. We report here the synthesis of four self-assembling peptide amphiphiles (PAs) containing a lysine ε-amine-derivatized hydrazide that was systematically placed at different positions along the backbone of the peptide sequence C 16V 2A 2E 2 (where C 16 = palmitic acid). Hydrazones were formed from each hydrazide by condensation with the solvatochromic dye 6-propionyl-2- dimethylaminonaphthalene (Prodan), which is typically used to probe cell membranes. All four compounds were found to self-assemble into nanofibers, and Prodan release was measured from filamentous gels prepared by screening PA charges with divalent cations. Near zero-order release kinetics were observed for all nanofibers, but release half-lives differed depending on the position of the fluorophore in the PA sequence. Dye release kinetics were rationalized through the use of cryogenic transmission electron microscopy, small-angle X-ray scattering, fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, and partition coefficient calculations. Relative release rates were found to correlate directly with fluorophore mobility, which varied inversely with packing density, degree of order in the hydrophobic PA core, and the β-sheet character of the peptide.

Original languageEnglish
Pages (from-to)3586-3595
Number of pages10
JournalSoft Matter
Volume8
Issue number13
DOIs
Publication statusPublished - Apr 7 2012

Fingerprint

Amphiphiles
Nanofibers
peptides
Nanostructures
drugs
Gels
gels
Peptides
Pharmaceutical Preparations
hydrazides
Fluorophores
Coloring Agents
dyes
palmitic acid
Hydrazones
fluorescence
hydrazones
Kinetics
Palmitic Acid
lysine

ASJC Scopus subject areas

  • Chemistry(all)
  • Condensed Matter Physics

Cite this

Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels. / Matson, John B.; Newcomb, Christina J.; Bitton, Ronit; Stupp, Samuel I.

In: Soft Matter, Vol. 8, No. 13, 07.04.2012, p. 3586-3595.

Research output: Contribution to journalArticle

Matson, John B. ; Newcomb, Christina J. ; Bitton, Ronit ; Stupp, Samuel I. / Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels. In: Soft Matter. 2012 ; Vol. 8, No. 13. pp. 3586-3595.
@article{7fb8cedae6264888941ee407cc158819,
title = "Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels",
abstract = "High aspect ratio peptide nanofibers have potential as biodegradable vehicles for drug delivery. We report here the synthesis of four self-assembling peptide amphiphiles (PAs) containing a lysine ε-amine-derivatized hydrazide that was systematically placed at different positions along the backbone of the peptide sequence C 16V 2A 2E 2 (where C 16 = palmitic acid). Hydrazones were formed from each hydrazide by condensation with the solvatochromic dye 6-propionyl-2- dimethylaminonaphthalene (Prodan), which is typically used to probe cell membranes. All four compounds were found to self-assemble into nanofibers, and Prodan release was measured from filamentous gels prepared by screening PA charges with divalent cations. Near zero-order release kinetics were observed for all nanofibers, but release half-lives differed depending on the position of the fluorophore in the PA sequence. Dye release kinetics were rationalized through the use of cryogenic transmission electron microscopy, small-angle X-ray scattering, fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, and partition coefficient calculations. Relative release rates were found to correlate directly with fluorophore mobility, which varied inversely with packing density, degree of order in the hydrophobic PA core, and the β-sheet character of the peptide.",
author = "Matson, {John B.} and Newcomb, {Christina J.} and Ronit Bitton and Stupp, {Samuel I}",
year = "2012",
month = "4",
day = "7",
doi = "10.1039/c2sm07420f",
language = "English",
volume = "8",
pages = "3586--3595",
journal = "Soft Matter",
issn = "1744-683X",
publisher = "Royal Society of Chemistry",
number = "13",

}

TY - JOUR

T1 - Nanostructure-templated control of drug release from peptide amphiphile nanofiber gels

AU - Matson, John B.

AU - Newcomb, Christina J.

AU - Bitton, Ronit

AU - Stupp, Samuel I

PY - 2012/4/7

Y1 - 2012/4/7

N2 - High aspect ratio peptide nanofibers have potential as biodegradable vehicles for drug delivery. We report here the synthesis of four self-assembling peptide amphiphiles (PAs) containing a lysine ε-amine-derivatized hydrazide that was systematically placed at different positions along the backbone of the peptide sequence C 16V 2A 2E 2 (where C 16 = palmitic acid). Hydrazones were formed from each hydrazide by condensation with the solvatochromic dye 6-propionyl-2- dimethylaminonaphthalene (Prodan), which is typically used to probe cell membranes. All four compounds were found to self-assemble into nanofibers, and Prodan release was measured from filamentous gels prepared by screening PA charges with divalent cations. Near zero-order release kinetics were observed for all nanofibers, but release half-lives differed depending on the position of the fluorophore in the PA sequence. Dye release kinetics were rationalized through the use of cryogenic transmission electron microscopy, small-angle X-ray scattering, fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, and partition coefficient calculations. Relative release rates were found to correlate directly with fluorophore mobility, which varied inversely with packing density, degree of order in the hydrophobic PA core, and the β-sheet character of the peptide.

AB - High aspect ratio peptide nanofibers have potential as biodegradable vehicles for drug delivery. We report here the synthesis of four self-assembling peptide amphiphiles (PAs) containing a lysine ε-amine-derivatized hydrazide that was systematically placed at different positions along the backbone of the peptide sequence C 16V 2A 2E 2 (where C 16 = palmitic acid). Hydrazones were formed from each hydrazide by condensation with the solvatochromic dye 6-propionyl-2- dimethylaminonaphthalene (Prodan), which is typically used to probe cell membranes. All four compounds were found to self-assemble into nanofibers, and Prodan release was measured from filamentous gels prepared by screening PA charges with divalent cations. Near zero-order release kinetics were observed for all nanofibers, but release half-lives differed depending on the position of the fluorophore in the PA sequence. Dye release kinetics were rationalized through the use of cryogenic transmission electron microscopy, small-angle X-ray scattering, fluorescence spectroscopy, fluorescence anisotropy, circular dichroism, and partition coefficient calculations. Relative release rates were found to correlate directly with fluorophore mobility, which varied inversely with packing density, degree of order in the hydrophobic PA core, and the β-sheet character of the peptide.

UR - http://www.scopus.com/inward/record.url?scp=84858032705&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84858032705&partnerID=8YFLogxK

U2 - 10.1039/c2sm07420f

DO - 10.1039/c2sm07420f

M3 - Article

VL - 8

SP - 3586

EP - 3595

JO - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 13

ER -