Serpin A1 Derivatives as Collagen Turnover Modulators for Cosmeceutical Uses

Errante, Fosca; Pascarella, Simona; Cipriani, Caterina; Giovannelli, Lisa; Papini, Anna Maria; Rovero, Paolo

doi:10.17952/35eps.2018.226

Cited by 1 publication

(2 citation statements)

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“…In particular, collagen levels in the lysates of cells treated with peptide AAT11RI were higher as compared to the other tested peptides, including the parent peptides AAT11, AAT11-allD, and SA1-III (Figures S3 and S4). Consequently, we focused on peptide AAT11RI, and further WB experiments confirmed that this peptide is able to significantly increase collagen concentration compared to that of CNTRL cells (Figure ).…”

Section: Resultsmentioning

confidence: 99%

“…The latter showed a surprisingly high activity when tested in vitro, in comparison with the parent peptides AAT11 and SA1-III. This is a remarkable observation as, generally speaking, despite a possible improved resistance to proteolytic degradation, the retro-inverso strategy does not necessarily lead to an increase in the activity. ,− Based on these preliminary results, peptide AAT11RI was patented . Further studies confirmed its activity in increasing collagen concentrations in vitro.…”

Section: Discussionmentioning

confidence: 99%

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Retro-Inverso Collagen Modulator Peptide Derived from Serpin A1 with Enhanced Stability and Activity In Vitro

Errante,

Pallecchi,

Bartolucci

et al. 2024

J. Med. Chem.

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The rising demand for novel cosmeceutical ingredients has highlighted peptides as a significant category. Based on the collagen turnover modulation properties of SA1-III, a decapeptide derived from a serine protease inhibitor (serpin A1), this study focused on designing shorter, second-generation peptides endowed with improved properties. A tetrapeptide candidate was further modified employing the retro-inverso approach that uses D-amino acids aiming to enhance peptide stability against dermal enzymes. Surprisingly, the modified peptide AAT11RI displayed notably high activity in vitro, as compared to its precursors, and suggested a mode of action based on the inhibition of collagen degradation. It is worth noting that AAT11RI showcases stability against dermal enzymes contained in human skin homogenates due to its rationally designed structure that hampers recognition by most proteases. The rational approach we embraced in this study underscored the added value of substantiated claims in the design of new cosmeceutical ingredients, representing a rarity in the field.

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Section: Resultsmentioning

confidence: 99%