Enhancement of plasma kallikrein specificity of antitrypsin variants identified by phage display and partial reversion

Pro substitution at P4 was found to be important for enhanced inhibition of Pka by AAT M358R. Two novel variants with this substitution are more rapid and selective inhibitors of Pka than AAT M358R and may provide better control of Pka in vivo than existing HAE therapeutics.

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Publication Details

Journal
BMC Biotechnology
Published
2025-03-12
DOI
https://doi.org/10.1186/s12896-025-00956-8
Citations
1
Primary Topic
Coagulation, Bradykinin, Polyphosphates, and Angioedema
Type
article
Field-Weighted Citation Impact
1.63

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article

Enhancement of plasma kallikrein specificity of antitrypsin variants identified by phage display and partial reversion

Toshiyuki Seto, Varsha Bhakta, Sangavi Sivananthan, William P. Sheffield et al.
1 citations
BMC Biotechnology
Coagulation, Bradykinin, Polyphosphates, and Angioedema
1.63
article

Enhancement of plasma kallikrein specificity of antitrypsin variants identified by phage display and partial reversion

Toshiyuki Seto, Varsha Bhakta, Sangavi Sivananthan, William P. Sheffield, Negin Chaechi Tehrani
article en
1 citations

Abstract

Pro substitution at P4 was found to be important for enhanced inhibition of Pka by AAT M358R. Two novel variants with this substitution are more rapid and selective inhibitors of Pka than AAT M358R and may provide better control of Pka in vivo than existing HAE therapeutics.

BMC BiotechnologyVol. 25(1)
Canadian Blood Services (CA), McMaster University (CA)
Canadian Blood Services
Zero hunger
Openalex Percentile: Top 19%
Coagulation, Bradykinin, Polyphosphates, and Angioedema
1.63
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