Hevea brasiliensis prohevein possesses a conserved C-terminal domain with amyloid-like properties in vitro

Highlights on Hevea brasiliensis (pro)hevein proteins

“…No hydrophobic core was observed [63]. The direct interaction of hevein (or prohevein) with lipids has never been observed [64]. Enzymatic activities have never been reported for hevein or prohevein [65].…”

“…Recombinant prohevein is also commercially available as a CCD-free recombinant protein (CDD, cross-reactive carbohydrate determinants; http://www.phadia.com). The crystal structure of prohevein has never been solved, but its potential structure has been investigated by modelling and ATR-FTIR [64]. The prediction model only encompasses the last 142 residues (Prohevein 37-187 ; Figure 3C), but suggests that the C-terminal domain may be organized as a β-barrel surrounded by small helices.…”

“…Anomalous staining and unexpected migration have often been reported, even using Tris-tricine gels with the "Schägger and von Jagow" protocol [43,61,64,[68][69][70]. Sharp bands may be difficult to observe and may require a large amount of proteins [46,64].…”

“…Prohevein was also purified from the B-serum by anion exchange chromatography [96,97]. It has been successfully purified and used as a tagged recombinant proteins (6xHis or MBP-rHev b 6.01) [35,42,64,91,98,99]. Dimers of recombinant prohevein may also be observed after purification [42,64], and prohevein may demonstrate auto-assembling and aggregative properties in vitro [64].…”

“…Hevein is now also commercially available as recombinant rHev b 6.02 [89,90] or may be purchased as a chemically synthesized peptide [64,91,92]. Additionally, hevein can adsorb to polymorphic calcium carbonate [93] and has also been shown to exhibit anti-aging properties on radiation vulcanized NR latex films [94] .…”