Self‐assembly of a conjugate of lipoic acid with a collagen‐stimulating pentapeptide showing cytocompatibility and wound healing properties, and chemical and photolytic disassembly

de Mello, L. R., Castelletto, V., Cavalcanti, L., Seitsonen, J. and Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2025) Self‐assembly of a conjugate of lipoic acid with a collagen‐stimulating pentapeptide showing cytocompatibility and wound healing properties, and chemical and photolytic disassembly. Journal of Peptide Science, 31 (3). e70002. ISSN 1099-1387 doi: 10.1002/psc.70002

Abstract/Summary

Lipoic acid is a biocompatible compound with antioxidant activity that is of considerable interest in cosmetic formulations, and the disulfide group in the N-terminal ring confers redox activity. Here, we study the self-assembly and aspects of the bioactivity of a lipopeptide (peptide amphiphile) comprising the KTTKS collagen-stimulating pentapeptide sequence conjugated to an N-terminal lipoic acid chain, lipoyl-KTTKS. Using SAXS, SANS and cryo-TEM, lipoyl-KTTKS is found to form a population of curly fibrils (wormlike micelles) above a critical aggregation concentration. Upon chemical reduction, the fibrils (and β-sheet structure) are disrupted because of the breaking of the disulfide bond, which produces dihydrolipoic acid. Lipoyl-KTTKS also undergoes photo-degradation in the presence of UV radiation. Through cell assays using fibroblasts, we found that lipoyl-KTTKS has excellent cytocompatibility across a wide concentration range, stimulates collagen production, and enhances the rate of cell coverage in a simple in vitro scratch assay of ‘wound healing’. Lipoyl-KTTKS thus has several notable properties that may be useful for the development of cosmetics, cell scaffolds or tissue engineering materials.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/120643
Item Type	Article
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	European Peptide Society and John Wiley & Sons
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