The papaya Kunitz-type trypsin inhibitor is a highly stable β-sheet glycoprotein

Azarkan, Mohamed; Dibiani, Rachid; Goormaghtigh, Erik; Raussens, Vincent; Baeyens‐Volant, Danielle

doi:10.1016/j.bbapap.2006.02.014

Cited by 71 publications

(71 citation statements)

References 38 publications

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“…The ajusted CD spectrum of the native ICTI with a negative band at approximately 201 nm ( Figure 5) showed that this PI is a β protein type composed by 40.4% of β-strand, 24.6% β-turn, 33% of unordered and 6.7% of α-helix secondary structures. This results are in accordance with most trypsin inhibitors particularly the Kunitz type inhibitors that are predominantly structurally organized in β-strand with little helical content (Azarkan et al 2006;Chaudhary et al 2008). Wavelength (nm) figure 5.…”

Section: Inga Cylindrica [Vell] Mart Seedssupporting

confidence: 69%

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Calderon

Filho

Teles

et al. 2010

Braz. J. Plant Physiol.

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Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds. ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (K i = 4.3 nM). Circular dichroism analysis revealed that this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors. ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by T m of 70. ) indicate a reduced structural stability of the protein under these conditions. This is likely to result from pK a differences of the acid and basic side chains reflecting the changes in the non-covalent interactions in the folded state.

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Section: Inga Cylindrica [Vell] Mart Seedssupporting

confidence: 69%

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Calderon

Filho

Teles

et al. 2010

Braz. J. Plant Physiol.

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“…PPI, however, has the amide group of the conserved asparagine substituted by the bulky side chain of a tyrosine, yet the protein remains a potent inhibitor of trypsin and -chymotrypsin (Azarkan et al, 2006;Odani et al, 1996). Moreover, the study of this molecule at atomic resolution will help us to understand how PPI is still capable of strongly inhibiting trypsin after previous incubation with an equimolar amount of -chymotrypsin and vice versa (Odani et al, 1996) and the apparent need for divalent metal ions for its inhibitory activity (Azarkan et al, 2006).…”

Section: Resultsmentioning

confidence: 99%

“…PPI was purified to high homogeneity using a combination of different chromatographic techniques: cation-exchange, hydrophobic interaction and thiophilic interaction chromatographies (Azarkan et al, 2004(Azarkan et al, , 2006. The purity of the sample was confirmed by the presence of a single band in a silver-stained SDS-PAGE and a single band in a Coomassie-blue stained isoelectric focusing gel.…”

Section: Resultsmentioning

confidence: 99%

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Crystallization and preliminary X-ray analysis of a protease inhibitor from the latex ofCarica papaya

et al. 2006

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A Kunitz-type protease inhibitor purified from the latex of green papaya (Carica papaya) fruits was crystallized in the presence and absence of divalent metal ions. Crystal form I, which is devoid of divalent cations, diffracts to a resolution of 2.6 Å and belongs to space group P3 1 or P3 2 . This crystal form is a merohedral twin with two molecules in the asymmetric unit and unit-cell parameters a = b = 74.70, c = 78.97 Å . Crystal form II, which was grown in the presence of Co 2+ , diffracts to a resolution of 1.7 Å and belongs to space group P2 1 2 1 2 1 , with unit-cell parameters a = 44.26, b = 81.99, c = 140.89 Å .

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“…It was also shown that some β -trefoil fold proteins (e.g., macrocypin, clitocypins, several lectins) are extremely resistant to extreme values of pH, proteolytic degradation, and exposure to high temperature (Kidrič et al, 2002 ;Gale š a et al, 2004 ;Azarkan et al , 2006 ;Sun et al , 2008 ), which makes them resistant to unfolding and digestion. It has already been shown that several β -trefoil inhibitors exhibit entomotoxic or insecticidal properties against several important crop pests and model insects where they can inhibit various digestive proteases (Lawrence and Koundal , 2002 ;Habib and Fazili , 2007 ;.…”

Section: Engineering β -Trefoil Inhibitorsmentioning

confidence: 99%

β-Trefoil inhibitors – from the work of Kunitz onward

Renko

Sabotič²,

Turk³

2012

Biological Chemistry

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Protein protease inhibitors are the tools of nature in controlling proteolytic enzymes. They come in different shapes and sizes. The β -trefoil protease inhibitors that come from plants, fi rst discovered by Kunitz, were later complemented with representatives from higher fungi. They inhibit serine (families S1 and S8) and cysteine proteases (families C1 and C13) as well as other hydrolases. Their versatility is the result of the plasticity of the loops coming out of the stable β -trefoil scaffold. For this reason, they display several different mechanisms of inhibition involving different positions of the loops and their combinations. Natural diversity, as well as the initial successes in de novo protein engineering, makes the β -trefoil proteins a promising starting point for the generation of strong, specifi c, multitarget inhibitors capable of inhibiting multiple types of hydrolytic enzymes and simultaneously interacting with different protein, carbohydrate, or DNA molecules. This pool of knowledge opens up new possibilities for the exploration of their naturally occurring as well as modifi ed properties for applications in many fi elds of medicine, biotechnology, and agriculture.

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The papaya Kunitz-type trypsin inhibitor is a highly stable β-sheet glycoprotein

Cited by 71 publications

References 38 publications

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Crystallization and preliminary X-ray analysis of a protease inhibitor from the latex ofCarica papaya

β-Trefoil inhibitors – from the work of Kunitz onward

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