Directed evolution towards protease-resistant hirudin variants.

doi:10.1016/j.ymgme.2003.09.007

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Article

Directed evolution towards protease-resistant hirudin variants.

Molecular genetics and metabolism - 1 Dec 2003

Wirsching Frank, Keller Martina, Hildmann Christian, Riester Daniel, Schwienhorst Andreas

Abstract excerpt

Hirudin, a thrombin-specific inhibitor, is efficiently digested and inactivated by proteases with pepsin- and chymotrypsin-like specificity. Using a combination of phage display selection and high-throughput screening methods, several variants of recombinant hirudin were generated. Only very few variants comprising amino acid substitutions in the amino-terminal domain (residues 1-5) and in the carboxyl-terminal...

Topics

Amino Acid Sequence
Bacteriophages
Base Sequence
Cloning, Molecular
Endopeptidases
Evolution, Molecular
Gene Library
Genetic Techniques
Hirudins
Humans
Inhibitory Concentration 50
Molecular Sequence Data
Mutation
Pepsin A
Protease Inhibitors
Thrombin

Source

Open in PubMed

Identifiers

PMID: 14654359
DOI: 10.1016/j.ymgme.2003.09.007

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