Assembly of an artificial protein hydrogel through leucine zipper aggregation and bisulfide bond formation

Assembly of an artificial protein hydrogel through leucine zipper aggregation and bisulfide bond formation
Engineering Village 2
2006 Elsevier Inc
Accession number: 05219120535

Title: Assembly of an artificial protein hydrogel through leucine zipper aggregation and bisulfide bond formation

Authors: Shen, Wei; Lammertink, Rob G.H.; Sakata, Jill K.; Kornfield, Julia A.; Tirrell, David A.

Author affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, United States

Serial title: Macromolecules

Abbreviated serial title: Macromolecules

Volume: v 38

Issue: n 9

Issue date: May 3 2005

Publication year: 2005

Pages: p 3909-3916

Language: English

ISSN: 0024-9297


Document type: Journal article (JA)

Publisher: American Chemical Society, Columbus, OH 43210-3337, United States

Abstract: We present a strategy to stabilize artificial protein hydrogels through covalent bond formation following physical association of terminal leucine zipper domains. Artificial proteins consisting of two terminal leucine zipper domains and a random coil central domain form transient networks above a certain concentration, but the networks dissolve when placed in excess buffer. Engineering of a cysteine residue into each leucine zipper domain allows formation of disulfide bonds templated by leucine zipper aggregation. Circular dichroism spectra show that the zipper domains remain helical after cysteine residues and disulfide bonds are introduced. Asymmetric placement of the cysteine residues in the leucine zipper domains suppresses intramolecular disulfide bonds and creates linked "multichains" composed of ca. 9 protein chains on average, as determined by multiangle light scattering measurements. These "multichains" act as the building units of the physical network formed by leucine zipper aggregation. The increased valency of the building units stabilizes the hydrogels in open solutions, while the physical nature of their association allows the reversibility of gelation to be retained. The gel networks dissolve at pH 12.2, where the helicity of the leucine zipper domains is reduced by ca. 90%, and re-form upon acidification. The hydrogels show anisotropic swelling when anchored on aminated surfaces and may find applications in tissue engineering, controlled release, and microarray technologies on the basis of their stability, reversibility, and swelling behavior. ? 2005 American Chemical Society.

Number of references: 39

Ei main heading: Proteins

Ei controlled terms: Hydrogels - Agglomeration - Chemical bonds - Gelation - pH effects - Dissolution - Rheology - Swelling - Light scattering

Uncontrolled terms: Artificial proteins - Acidification - Anisotropic swelling - Tissue engineering

Ei classification codes: 804.1 Organic Compounds - 801.3 Colloid Chemistry - 802.3 Chemical Operations - 801.4 Physical Chemistry - 801.1 Chemistry, General - 931.1 Mechanics - 741.1 Light/Optics

Treatment: Theoretical (THR); Experimental (EXP)

DOI: 10.1021/ma048348s

Database: Compendex

Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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