Cited by 8Protease and Inhibitor MechanismsProtein Structure and DynamicsProtein Interaction Studies and Fluorescence Analysis

Kinetic and equilibrium characterization of the interaction between bovine trypsin and I-ovalbumin

Cuccioloni, Massimiliano, Sparapani, Luca, Amici, Manila, Lupidi, Giulio, Eleuteri, Anna Maria, Angeletti, Mauro·2004·Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Abstract

Serpins are a superfamily of structurally linked proteins with interesting functional properties. Most serpins act as proteinase suicide inhibitors and play a key role in a number of physiological processes. Structural flexibility properties make serpins extremely available to conformational transitions, often causing changes in protein function. Ovalbumin is a member of the serpin family that is not able to inhibit serine proteinases in its native form. In contrast, I-ovalbumin, the product of a heating transition, is a potent reversible serine proteinase inhibitor. In this paper, a detailed equilibrium and kinetic characterization of the interaction between the serpin ovalbumin and bovine trypsin, using a resonant mirror technique, is reported. This methodology revealed that the high affinity interaction between the two binding partners is characterized by high kinetic association constants and low kinetic dissociation constants. The modulation exerted by protons in solution, examined taking into account structural motifs characterizing the binding interface between the two macromolecules, suggests an interaction reminiscent of that observed for the binding of other serine proteases to their ligands.

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Crossref · 10.1016/j.bbapap.2004.08.019

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Authors
Cuccioloni, M., Sparapani, L., Amici, M., Lupidi, G., Eleuteri, A. M., & Angeletti, M.
Affiliations
Università di Camerino (IT)
Corresponding author
Cuccioloni, Massimiliano
Venue
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Publisher
Elsevier BV
Published
2004-11
Volume
1702
Issue
2
Pages
199-207
ISSN
1570-9639 (ISSN-L)
OpenAlex
W2035492984
Cited by
8
References
63
Citations by year
2025: 1 · 2017: 2 · 2014: 1
FWCI
0.41
Type
journal article
Language
en
Open access
closed
Locations
  • Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (publishedVersion)
  • PubMed (publishedVersion)
  • Unicam Scientific Publications (University of Camerino) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Keywords
bovine trypsin, serpins, serine protease inhibitors, protein-protein interaction kinetics, binding equilibrium, proton modulation, binding interface
MeSH terms
Animals, Cattle, Chickens, Hydrogen-Ion Concentration, Models, Theoretical, Ovalbumin, Protein Binding, Trypsin, Biosensing Techniques, Serine Proteinase Inhibitors, Surface Plasmon Resonance

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