A Light Scattering Investigation of Enzymatic Gelation in Self-Assembling Peptides

Author:

Buzzaccaro Stefano1ORCID,Ruzzi Vincenzo1ORCID,Gelain Fabrizio23ORCID,Piazza Roberto1ORCID

Affiliation:

1. Department of Chemistry, Materials Science, and Chemical Engineering (CMIC), Politecnico di Milano, Edificio 6, Piazza Leonardo da Vinci 32, 20133 Milano, Italy

2. Unità di Ingegneria Tissutale, Fondazione IRCCS Casa Sollievo della Sofferenza, 71013 San Giovanni Rotondo, Italy

3. Center for Nanomedicine and Tissue Engineering, ASST GOM Niguarda, 20162 Milano, Italy

Abstract

Self-assembling peptides (SAPs) have been increasingly studied as hydrogel–former gelators because they can create biocompatible environments. A common strategy to trigger gelation, is to use a pH variation, but most methods result in a change in pH that is too rapid, leading to gels with hardly reproducible properties. Here, we use the urea–urease reaction to tune gel properties, by a slow and uniform pH increase. We were able to produce very homogeneous and transparent gels at several SAP concentrations, ranging from c=1g/L to c=10g/L. In addition, by exploiting such a pH control strategy, and combining photon correlation imaging with dynamic light scattering measurements, we managed to unravel the mechanism by which gelation occurs in solutions of (LDLK)3-based SAPs. We found that, in diluted and concentrated solutions, gelation follows different pathways. This leads to gels with different microscopic dynamics and capability of trapping nanoparticles. At high concentrations, a strong gel is formed, made of relatively thick and rigid branches that firmly entrap nanoparticles. By contrast, the gel formed in dilute conditions is weaker, characterized by entanglements and crosslinks of very thin and flexible filaments. The gel is still able to entrap nanoparticles, but their motion is not completely arrested. These different gel morphologies can potentially be exploited for controlled multiple drug release.

Funder

The Italian Ministry of University and Research

Publisher

MDPI AG

Subject

Polymers and Plastics,Organic Chemistry,Biomaterials,Bioengineering

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