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Macromolecular diffusion and release from self-assembled β-hairpin peptide hydrogels

Paper ID Volume ID Publish Year Pages File Format Full-Text
9180 619 2009 9 PDF Available
Title
Macromolecular diffusion and release from self-assembled β-hairpin peptide hydrogels
Abstract

Self-assembling peptide hydrogels are used to directly encapsulate and controllably release model FITC–dextran macromolecules of varying size and hydrodynamic diameters. MAX1 and MAX8 are two peptide sequences with different charge states that have been designed to intramolecularly fold and self assemble into hydrogels at physiological buffer conditions (pH 7.4, 150 mm NaCl). When self-assembly is initiated in the presence of dextran or protein probes, these macromolecules are directly encapsulated in the gel. Self-diffusion studies using fluorescence recovery after photobleaching (FRAP) and bulk release studies indicate that macromolecule mobility within, and release out of, these gels can be modulated by varying the hydrogel mesh size. The average mesh size can be modulated by simply varying the concentration of a given peptide used to construct the gel or by altering the peptide sequence. In addition, results suggest that electrostatic interactions between the macromolecules and the peptide network influence mobility and release. Depending on probe size, release half-lives can be varied from 8 h to over a month.

Keywords
Hydrogel; Delivery; Self-assembly; Peptide
First Page Preview
Macromolecular diffusion and release from self-assembled β-hairpin peptide hydrogels
Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 30, Issue 7, March 2009, Pages 1339–1347
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering