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Drug Week
September 11, 2009
ENZYME RESEARCH;
Scientists at Institute of Biotechnology target enzyme research
Data detailed in 'The novel inhibitors of serine proteases' have been
presented. According to a study from Yerevan, Armenia, "Thirty
optically active nonprotein alpha-amino acids and peptides based
thereon have been screened for their ability to interact with bovine
trypsin and proteinase K from Tritirachium album Limber, which belong
to the group of serine proteases. Both structure-based drug design
approach and determination of enzyme activity have been used to
identify low molecular weight inhibitors of trypsin and proteinase K."
"Compounds have been selected that according to the docking analysis
were able to interact with trypsin and proteinase K. Following the
docking analysis measurement of enzymes activity
(2R,3S)-beta-hydroxyleucine and (2S,3R)-beta-hydroxyleucine inhibited
both enzymes activity, whereas (S)-alpha-methyl-beta-phenylalanine,
®-alpha- methyl-beta-phenylalanine, (S)-allylglycine, ®-allylglycine,
(S)-alpha-allylalanine, ®-alpha-allylalanine and allo-O-ethylthreonine
inhibited only proteinase K; and
N-formyl-(S)-methionyl-(2S,3R)-hydroxyleucine,
N-formyl-(S)-methionyl-(2R,3S)-hydroxyleucine,
N- formyl-(S)-methionyl-(S)-allylglycine and
N-formyl-(S)-methionyl-®-allylglycine inhibited trypsin," wrote
N. Hovhannisyan and colleagues, Institute of Biotechnology (see also
Enzyme Research).
The researchers concluded: "It has been shown that inhibition of
trypsin by (2R,3S)-beta-hydroxyleucine and
N-formyl-(S)-methionyl-(2R,3S)-hydroxyleucine is of a competitive
mode."
Hovhannisyan and colleagues published their study in Amino Acids (The
novel inhibitors of serine proteases. Amino Acids, 2009;37(3):531-6).
For more information, contact N. Hovhannisyan, Institute of
Biotechnology, Yerevan, Armenia.
Publisher contact information for the journal Amino Acids is:
Springer, 233 Spring Street, New York, NY 10013, USA.
September 11, 2009
ENZYME RESEARCH;
Scientists at Institute of Biotechnology target enzyme research
Data detailed in 'The novel inhibitors of serine proteases' have been
presented. According to a study from Yerevan, Armenia, "Thirty
optically active nonprotein alpha-amino acids and peptides based
thereon have been screened for their ability to interact with bovine
trypsin and proteinase K from Tritirachium album Limber, which belong
to the group of serine proteases. Both structure-based drug design
approach and determination of enzyme activity have been used to
identify low molecular weight inhibitors of trypsin and proteinase K."
"Compounds have been selected that according to the docking analysis
were able to interact with trypsin and proteinase K. Following the
docking analysis measurement of enzymes activity
(2R,3S)-beta-hydroxyleucine and (2S,3R)-beta-hydroxyleucine inhibited
both enzymes activity, whereas (S)-alpha-methyl-beta-phenylalanine,
®-alpha- methyl-beta-phenylalanine, (S)-allylglycine, ®-allylglycine,
(S)-alpha-allylalanine, ®-alpha-allylalanine and allo-O-ethylthreonine
inhibited only proteinase K; and
N-formyl-(S)-methionyl-(2S,3R)-hydroxyleucine,
N-formyl-(S)-methionyl-(2R,3S)-hydroxyleucine,
N- formyl-(S)-methionyl-(S)-allylglycine and
N-formyl-(S)-methionyl-®-allylglycine inhibited trypsin," wrote
N. Hovhannisyan and colleagues, Institute of Biotechnology (see also
Enzyme Research).
The researchers concluded: "It has been shown that inhibition of
trypsin by (2R,3S)-beta-hydroxyleucine and
N-formyl-(S)-methionyl-(2R,3S)-hydroxyleucine is of a competitive
mode."
Hovhannisyan and colleagues published their study in Amino Acids (The
novel inhibitors of serine proteases. Amino Acids, 2009;37(3):531-6).
For more information, contact N. Hovhannisyan, Institute of
Biotechnology, Yerevan, Armenia.
Publisher contact information for the journal Amino Acids is:
Springer, 233 Spring Street, New York, NY 10013, USA.