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Binding effect of proline-rich-proteins (PRPs) on in vitro antimicrobial activity of the flavonoids

The interaction of the cyanidin, pelargonidin, catechin, myrecetin and kaempferol with casein and gelatin, as proline rich proteins (PRPs), was studied. The binding constants calculated for both flavonoid-casein and flavonoid-gelatin were fairly large (105–107 M−1) indicating strong interaction. Due to higher proline content in gelatin, the binding constants of flavonoid-gelatin (2.5 × 105–6.2 × 107M−1) were found to be higher than flavonoid-casein (1.2 × 105–5.0 × 107 M−1). All the flavonoids showed significant antibacterial activity against the tested strains. Significant loss in activity was observed due to the complexation with PRPs confirming that binding effectively reduced the concentration of the free flavonoids to be available for antibacterial activity. The decline in activity was corresponding to the values of the binding constants. Though the activities of free catechin and myrecetin were higher compared to pelargonidin, cyanidin and kaempferol yet the decline in activity of catechin and myrecetin due to complexation with casein and gelatin was more pronounced.

proline rich proteins; flavonoids; catechin; myrecetin; kaempferol; pelargonidin; cyanidin; gelatin; casein; binding constants


Sociedade Brasileira de Microbiologia USP - ICB III - Dep. de Microbiologia, Sociedade Brasileira de Microbiologia, Av. Prof. Lineu Prestes, 2415, Cidade Universitária, 05508-900 São Paulo, SP - Brasil, Ramal USP 7979, Tel. / Fax: (55 11) 3813-9647 ou 3037-7095 - São Paulo - SP - Brazil
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