药剂师
四肽
化学
舍宾
蛋白酵素
肽
体外
合理设计
蛋白酶
生物化学
酶
丝氨酸蛋白酶
丝氨酸
体外毒理学
纳米技术
生物
基因
材料科学
生物技术
作者
Fosca Errante,Marco Pallecchi,Gianluca Bartolucci,Elena Frediani,Francesca Margheri,Lisa Giovannelli,Anna Maria Papini,Paolo Rovero
标识
DOI:10.1021/acs.jmedchem.4c00137
摘要
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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