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Suitability of high‐molecular‐weight tissue‐derived elastin polypeptides and their particles as cosmetic biomaterials.

Authors :
Sakai, Toma
Sodemoto, Nanami
Inoue, Asako
Taniguchi, Suguru
Maeda, Iori
Hikima, Tomohiro
Source :
Journal of Peptide Science; Jun2023, Vol. 29 Issue 6, p1-8, 8p
Publication Year :
2023

Abstract

We aimed to determine the coacervation properties of high‐molecular‐weight (HMW) tissue‐derived elastin (TDE) and to examine the potential use of TDE particles as a cosmetic biomaterial. TDE solutions were filtered and divided into three fractions (1–3) according to the molecular weight of the elastin. The turbidity of fraction 2, which contained a large portion (58%) of HMW elastin polypeptides (>100 kDa), was measured under several pH values (3.0–11.0) and NaCl concentrations (0–1000 mM) to examine its coacervation ability. HMW TDE exhibited coacervation under the physiological conditions (temperature, pH, and NaCl concentration) of the skin surface. We performed inclusion and release experiments using three model chemicals with different molecular weights and measured the size and zeta potential of the fraction 3 particles to investigate the suitability of HMW elastin polypeptides. Fraction 3, which contained a larger portion (64%) of HMW elastin polypeptides, displayed a strong coacervation property at a phase transition temperature of 19.8 ± 0.1°C. The inclusion ratio of the model chemical Biebrich Scarlet (BS) with a molecular weight of <600 was approximately 92.1 ± 0.7%. The release profiles of BS from the particles linearly increased and reached a plateau after 15 days. Moreover, the average size of the particles with BS was 474.2 ± 24.6 nm. The low‐molecular‐weight (LMW) elastin peptides have moisturizing and whitening functions for the skin. We concluded that TDE, as a mixture of HMW polypeptides and LMW peptides, can potentially serve as a multifunctional and effective cosmetic biomaterial. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10752617
Volume :
29
Issue :
6
Database :
Complementary Index
Journal :
Journal of Peptide Science
Publication Type :
Academic Journal
Accession number :
163588838
Full Text :
https://doi.org/10.1002/psc.3472