Advanced search

Lysine containing amphiphilic peptide-based non-cytotoxic soft materials with potential antifungal and antibacterial activities for 3D cell culture

Download
[thumbnail of BanerjeeManuscriptSoftMatter.docx]
Text
· Restricted to Repository staff only
· The Copyright of this document has not been checked yet. This may affect its availability.
Advice

Please see our End User Agreement.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

Tools
Add to AnyAdd to TwitterAdd to FacebookAdd to LinkedinAdd to PinterestAdd to Email
Lists

Banerjee, S., Haldar, S., Bose, S., Chatterjee, S., Castelletto, V., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Sinha, D. K. and Banerjee, A. ORCID: https://orcid.org/0000-0002-1309-921X (2026) Lysine containing amphiphilic peptide-based non-cytotoxic soft materials with potential antifungal and antibacterial activities for 3D cell culture. Soft Matter, 22 (20). pp. 3662-3673. ISSN 1744-683X doi: 10.1039/d6sm00190d

Abstract/Summary

Two amphiphilic peptides each with an N-terminal lysine residue have been designed and synthesized. These self-assembling peptide-based molecules form transparent hydrogels in Tris-HCl buffer at physiological pH. Transmission electron microscopic (TEM) images of the peptide hydrogels reveal a nanofibrillar network. Rheological studies reveal high values of storage moduli for these two enantiomeric peptide hydrogels, demonstrating high mechanical strength. Interestingly, these peptide hydrogels exhibit potential antibacterial properties against multidrug-resistant bacterial strains and antifungal activities with great efficacy. The gelators are cytocompatible with NIH 3T3 and HEK 293 cells. The peptide gelator containing D-amino acid residues displayed excellent proteolytic stability against chymotrypsin, pepsin, and proteinase K. The peptide-based hydrogels were successfully used as a suitable platform for 3-dimensional cell culture, pointing to future applications in regenerative medicine, which, combined with their antimicrobial properties, holds promise for the discovery of new peptide based biomaterials in biomedicine.

Altmetric Badge

Dimensions Badge

Item Type Article
URI https://centaur.reading.ac.uk/id/eprint/130004
Identification Number/DOI 10.1039/d6sm00190d
Refereed Yes
Divisions Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher Royal Society of Chemistry
Download/View statistics View download statistics for this item
Deposit Details
CORE (COnnecting REpositories)

University Staff: Request a correction | Centaur Editors: Update this record