[Hydrophobic interactions of serine proteases with low molecular compounds: role of the S'2-site in substrate activation and interaction with serpines].
An attempt is made to simulate the P1-P'2 site of the reactive centre of protein inhibitors of serine proteases (serpines). On the basis of data from literature structure requirements are formulated and compound 1,5 bis-dibenzyl-aminopentane is synthesized. It may simultaneously interact with S1- and S'2-sites of chymotrypsin and contains no bonds adequate to the hydrolytic centre of proteinase. The compound is studied for its effect on hydrolysis of low-molecular substrates and proteins by chymotrypsin. Results obtained are discussed as well as the possible role of the S'2-binding site in the substrate activation of serine proteinases and their interaction with serpines.
Verevka
S V
SV
Shulezhko
L A
LA
Kolodzeĭskaia
M V
MV
D001665:Binding Sites / Q000502:physiology; D002918:Chymotrypsin / Q000378:metabolism; D006868:Hydrolysis; D008970:Molecular Weight; D015842:Serine Proteinase Inhibitors / Q000378:metabolism*; D014867:Water
D015842:Serine Proteinase Inhibitors; D014867:Water; D002918:Chymotrypsin
Gidrofobnye vzaimodeĭstviia serinovykh proteaz s nizkomolekuliarnymi soedineniiami: rol' S'2-uchastka v substratnoĭ aktivatsii i vzaimodeĭstvii s serpinami.