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Serpin A1 C‐Terminal Peptides as Collagen Turnover Modulators
Author(s) -
Pascarella Simona,
Tiberi Caterina,
Sabatino Giuseppina,
Nuti Francesca,
Papini Anna Maria,
Giovannelli Lisa,
Rovero Paolo
Publication year - 2016
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201500472
Subject(s) - serpin , chemistry , context (archaeology) , type i collagen , biochemistry , in vitro , microbiology and biotechnology , biology , endocrinology , gene , paleontology
The modulation of collagen turnover can be a relevant pharmacological target in the context of treating either pathological or pathophysiological conditions, such as collagen‐related diseases and skin aging. Our recent work has focused on the search for short‐chain peptides as lead compounds for further development of compounds that enhance the production of type I collagen. In this study we selected and synthesized overlapping peptides of the C‐terminal portion of serpin A1 (residues 393–418), the impact of which on collagen production has been reported previously, in order to identify shorter and still active fragments and to provide insight on the mechanisms involved. The biological activity of each fragment was evaluated with cultured normal human dermal fibroblasts, and changes in the amounts of collagen were monitored in collected culture media by a sandwich ELISA technique developed in house. Interestingly, we identified a decapeptide, termed SA1‐III (Ac‐MGKVVNPTQK‐NH 2 ), as a promising candidate for our purposes; it is able to induce a significant increase in type I collagen levels in the culture medium of treated cells at micromolar concentrations.