PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9154941-3	1997	In order to characterize the interaction, NMR studies were performed which involved titrating a series of polyphenols into a synthetic 19-residue PRP fragment.	Polyphenols	106-117	prion protein	Homo sapiens	146-149	
9154941-5	1997	Measurement of dissociation constants indicates that the larger and more complex polyphenols interact more strongly with the PRP fragment; the order of binding affinity was determined as procyanidin dimer B-2 > pentagalloylglucose > trigalloylglucose >> proanthocyanidin monomer (-)-epicatechin approximately propyl gallate.	Polyphenols	81-92	prion protein	Homo sapiens	125-128	
9154941-7	1997	The more complex polyphenols interact with the PRP fragment in a multidentate fashion; moreover, they self-associate or stack when bound.	Polyphenols	17-28	prion protein	Homo sapiens	47-50	
9154941-8	1997	Thus, a model is proposed in which multiple polyphenol/polyphenol and polyphenol/PRP interactions act cooperatively to achieve precipitation.	Polyphenols	44-54	prion protein	Homo sapiens	81-84