@article {pina_studies_2009,
	title = {Studies on the molecular recognition between bioactive peptides and angiotensin-converting enzyme},
	journal = {Journal of Molecular Recognition},
	volume = {22},
	number = {2},
	year = {2009},
	note = {<p>{PMID:} 18816584</p>
},
	month = {apr},
	pages = {162{\textendash}168},
	abstract = {<p>High blood pressure or hypertension is a condition affecting many individuals and represents a controllable risk factor for cardiovascular diseases such as coronary heart disease and stroke. A non-pharmacological approach to manage these includes the application of food components with antihypertensive activity. Milk protein-derived peptides have been exploited as natural hypotensive agents, namely the peptides {Val-Pro-Pro} {(VPP)} and {Ile-Pro-Pro} {(IPP)}, already commercialized in functional foods as a potential alternative to synthetic drugs. These bioactive peptides inhibit in vitro and in vivo the Angiotensin I-converting enzyme {(ACE)}, a protein with an important role in blood pressure regulation. In this work, we attempted to elucidate the possible mode of interaction between the peptides and {ACE}, including mechanisms of binding to the cofactor Zn2+, and further contrast this with the known mode of inhibition exerted by synthetic drugs {(Captopril}, Enalaprilat and Lisinopril). The bioactive peptide {Ala-Leu-Pro-Met-His-Ile-Arg} {(ALPMHIR)}, also known to inhibit the enzyme {ACE} but with a lower efficiency than {VPP} and {IPP}, was utilized in the docking studies for comparison. It was observed that the best docking poses obtained for {VPP} and {IPP} were located at the {ACE} catalytic site with very high resemblance to the drugs mode of interaction, including the coordination with Zn2+. As for {ALPMHIR}, the best docking poses were located in the narrow {ACE} channel outside the catalytic site, representing higher affinity energies and fewer resemblances with the interaction established by drugs.</p>
},
	keywords = {Catalytic Domain, Crystallography, Humans, Hydrogen Bonding, Milk Proteins, Oligopeptides, Protein Binding, Protein Conformation, Zinc, {Angiotensin-Converting} Enzyme Inhibitors, {Peptidyl-Dipeptidase} A, {X-Ray}},
	issn = {0952-3499},
	doi = {10.1002/jmr.905},
	url = {http://www.ncbi.nlm.nih.gov/pubmed/18816584},
	author = {Pina, A. S. and Roque, A. C. A.}
}
