Related Experiment Video
Updated: May 9, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
Published on: September 6, 2024
Rheology and morphology of pristine graphene/polyacrylamide gels
Sriya Das1, Fahmida Irin, Lan Ma
1Department of Chemical Engineering, Texas Tech University , Lubbock, Texas 79409, United States.
Abstract:
Enhancement of toughness in nanomaterial-based hydrogels is a critical metric for many of their engineering applications. Pristine graphene-polyacrylamide (PAM) hydrogels are synthesized via in situ polymerization of acrylamide monomer in PAM-stabilized graphene dispersion. In-situ polymerization leads to the uniform dispersion of the graphene sheets in the hydrogel. The graphene sheets interact with the elastic chains of the hydrogel through physisorption and permit gelation in the absence of any chemical cross-linker. This study represents the first report of pristine graphene as a physical cross-linker in a hydrogel. The properties of the graphene-polymer hydrogel are characterized by rheological measurements and compressive tests, revealing an increase in the storage modulus and toughness of the hydrogels compared to the chemically cross-linked PAM analogues. The physically cross-linked graphene hydrogels also exhibit self-healing properties. These hydrogels prove to be efficient precursors for graphene-PAM aerogels with enhanced electrical conductivity and thermal stability.
Related Concept Videos
Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...

