Human α1-antitrypsin (hAAT), a member of the Serine Protease Inhibitors (SERPIN) super family, is the third most abundant circulating protein in humans. While known for its ability to inhibit elastase and other serine proteases. Given its affiliation with the SERPIN super family, it was originally assumed that the hAAT deficiency results from a protease:anti-protease imbalance that leads to uncontrolled protease activity and to tissue damage. However, it was shown that the lack of the ability to block proteases is not correlated with hAAT’s immunoregulatory and cytoprotective functions. In addition, hAAT’s inflammation-modulatory properties were also detected in hAAT chimeric proteins lacking anti-protease activity, further supporting the hypothesis that the anti-protease and anti-inflammatory activities may be independent and mediated by different structural domains of hAAT. Based on in silico approach we identified biologically active immunoregulatory sites on hAAT surface that are not associated with its anti-protease activity. Using peptide/peptidomimetic chemistry, we plan develop therapeutic metabolically stable peptides that could be used as a basis for developing of novel wound healing drug candidates as a topical treatment. The presented approach (the peptide derived from hAAT site that is not associated with canonical anti-protease activity) is totally novel.