Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges

Vincent, Jean Pierre; Lazdunski, Michel

doi:10.1021/bi00766a007

Cited by 264 publications

(202 citation statements)

References 25 publications

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“…Interestingly, using volumes to obtain ASP values (cal/A3) produces the best correlation, suggesting that cavity formation is an important parameter in calculating the free The experimental association energies were obtained from the literature. a, Vincent and Lazdunski (1972); b, Vincent et al (1974); c, Chen and Bode (1983); d, Hass and Ryan (1980); e, Bunting and Myers (1975); f, Read et al (1983); g, Ascenzi et al (1988); h, Empie and Laskowski (1982); i, Bode (1979) and Bolognes et al (1982); j , Pekar and Frank (1972); k , Akasaka et al (1982); I, Sheriff et al (1987); m, Ross et al (1977). Chothia and Janin (1975) first suggested that the free energy of association was related to the amount of surface area that was buried in the interface.…”

Section: Resultsmentioning

confidence: 99%

Calculation of the free energy of association for protein complexes

1992

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We have developed a method for calculating the association energy of quaternary complexes starting from their atomic coordinates. The association energy is described as the sum of two solvation terms and an energy term to account for the loss of translational and rotational entropy. The calculated solvation energy, using atomic solvation parameters and the solvent accessible surface areas, has a correlation of 96% with experimentally determined values. We have applied this methodology to examine intermediates in viral assembly and to assess the contribution isomerization makes to the association energy of molecular complexes. In addition, we have shown that the calculated association can be used as a predictive tool for analyzing modeled molecular complexes.Keywords: hydrophobicity; protein structure; solvation Specific interactions between macromolecules are responsible for the assembly of complex biological structures and are essential to the regulation of events within a cell or organism. The association of molecules to form higher ordered oligomers is in many respects analogous to the block condensation model for protein folding where prefolded units associate to form higher order structures (Richmond & Richards, 1978). To understand the structural basis of recognition we must be able to relate solution measurements of the association process to the structure of the macromolecular complex. This paper considers the problem of calculating the free energies of forming protein complexes from preformed subunits as derived from crystallographic data and relating these values to experimentally obtained association constants. Kauzmann (1959) suggested that a major factor in the stable formation of protein complexes is a consequence of the hydrophobic effect. Using an empirical correlation between the accessible surface area and free energies of transfer of amino acids from water to octanol, Chothia and Janin (1975) found that the free energy required to form a stable complex was directly related to the amount of surface area buried in the interface. Eisenberg and McLachlan (1986) recognized that it is an oversimplificaReprint requests to: Mitchell Lewis, The Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104. tion to base the energy of association on surface area alone; polarity and charge must also be considered. By introducing five atomic solvation parameters, to account for the polar or apolar character of each atom type most frequently found in proteins, they could more accurately relate surface area to the free energy of transfer. Moreover, the solvation energy was shown to be useful for assessing protein stability. We assume that the forces that govern the association between two molecules are the same as the forces that are responsible for the folding of a protein in water. As such, the solvation energy should be equally useful as a gauge for evaluating the association energies of quaternary structu...

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Section: Resultsmentioning

confidence: 99%

Calculation of the free energy of association for protein complexes

1992

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“…raM), and measured spectrophotometncally at 324 nm. q'hl~ association was al~o measured by competition experiments using active site thrated chymotrypsm as the ~econd enzyme besides PR3 [14,15].…”

Section: Htteractwn El Ph)moioew Mhtbitors With Pr3mentioning

confidence: 99%

“…This experiment was used to determine the ~2M coneentiauon a~umm~ the molar binding ratio of PR3 to ~:M is I'1 [5,16]. The a~soeiation rate constant of PR3 with ~,M was measured compeutively with ~etAT [14,16]. PR3 (I 1.5 nM) was added to a mixture of ~t,M (12.8 nM) and various amounts of chAT (11.5-57.6 nM) in 0.5 M NaCl, 0 1 M HEPES, pH 7.5, at 25°C.…”

Section: Htteractwn El Ph)moioew Mhtbitors With Pr3mentioning

confidence: 99%

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Determination of proteinase 3—α₁‐antitrypsin complexes in inflammatory fluids

et al. 1992

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Phy~iological inht biters were tested for their in vitro interaction with neutrophil protemase 3 (PR3). The major plasma protemase inhibitor of PR3 is =tAT. We have developed a radioimmunoa~ay (RIA) for quantitative detection of PR3--CtlAT complexes formed in rive in inflammatory exudates such as synovtal fluid and plasma from patients with sepsis. Levels ofPR3-a~AT complexeb correlated significantly with levels of human nemrophtl elastase (HNE)--~tAT complexes. Thus, in vtvo a~AT not only proteet~ against excessive HNE activity, but also against excessive PR3 activity.

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“…Protease inhibitors have a wider range of activity than Bt proteins, binding to the digestive proteases of many insects (Terra and Ferreira, 1994). The similar binding domains of BPTI and BSTI (Fioretti et al, 1985) cause these inhibitors to bind more strongly to bovine digestive trypsin than any other known PI-protease interaction (Vincent and Lazdunski, 1972), suggesting that these inhibitors have greater potential for impacting non-target organisms that utilize proteases in their digestive systems than other insecticidal compounds with a similar mode of action. BSTI is therefore a good candidate for detection of any such impacts.…”

Section: Introductionmentioning

confidence: 99%

Effects of tobacco genetically modified to express protease inhibitor bovine spleen trypsin inhibitor on non-target soil organisms

O’Callaghan

Brownbridge

Stilwell

et al. 2007

Environ. Biosafety Res.

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Effects of tobacco genetically modified to express the protease inhibitor bovine spleen trypsin inhibitor (BSTI) were examined in laboratory assays against three earthworm and one collembolan species. BSTI is a serine protease inhibitor that can bind to the digestive trypsins of insects feeding on modified plants, resulting in reduced growth and survival. Protease inhibitors are active against a broad range of insects, so may have a large impact on non-target organisms. Survival and fecundity of the collembolan Folsomia candida were unaffected by consumption of artificial diet containing BSTI-expressing tobacco leaf or powdered freeze-dried BSTI-expressing tobacco leaf that was added to soil. Similarly, mortality and growth of earthworms Aporrectodea caliginosa and Lumbricus rubellus did not differ significantly between soil augmented with BSTI-expressing tobacco leaves or unmodified control leaves. The redworm Eisenia fetida gained less weight when provided with BSTI-expressing leaves in one assay, but when the experiment was repeated, there was no significant difference between treatments. BSTI-expressing tobacco and unmodified control leaves decomposed at the same rate, indicating that the inhibitor had no effect on the overall function of the decomposer community of micro-flora and fauna in soil.

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Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges

Cited by 264 publications

References 25 publications

Calculation of the free energy of association for protein complexes

Calculation of the free energy of association for protein complexes

Determination of proteinase 3—α₁‐antitrypsin complexes in inflammatory fluids

Effects of tobacco genetically modified to express protease inhibitor bovine spleen trypsin inhibitor on non-target soil organisms

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Trypsin-pancreatic trypsin inhibitor association. Dynamics of the interaction and role of disulfide bridges

Cited by 264 publications

References 25 publications

Calculation of the free energy of association for protein complexes

Calculation of the free energy of association for protein complexes

Determination of proteinase 3—α1‐antitrypsin complexes in inflammatory fluids

Effects of tobacco genetically modified to express protease inhibitor bovine spleen trypsin inhibitor on non-target soil organisms

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Determination of proteinase 3—α₁‐antitrypsin complexes in inflammatory fluids