Synthesis and Structure−Activity Relationships of Linear and Conformationally Constrained Peptide Analogues of CIYKYY as Src Tyrosine Kinase Inhibitors

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DC Field	Value	Language
dc.contributor.author	Kumar, Anil	-
dc.date.accessioned	2021-10-27T04:11:55Z	-
dc.date.available	2021-10-27T04:11:55Z	-
dc.date.issued	2006-04-29	-
dc.identifier.uri	https://pubs.acs.org/doi/10.1021/jm060334k	-
dc.identifier.uri	http://dspace.bits-pilani.ac.in:8080/xmlui/handle/123456789/2956	-
dc.description.abstract	A series of peptide analogues of Ac-CIYKYY (1) were synthesized by functional group modifications in peptide side chains or by introducing conformational constraints, to improve the inhibitory potency against active Src kinase. Ac-CIYKF(4-NO2)Y (2, IC50 = 0.53 μM) and conformationally constrained peptide 31 (IC50 = 0.28 μM) exhibited 750- and 1400-fold higher inhibitory activities, respectively, versus that of 1 (IC50 = 400 μM). Compound 2 exhibited a partial competitive inhibition pattern against ATP.	en_US
dc.language.iso	en	en_US
dc.publisher	ACS	en_US
dc.subject	Chemistry	en_US
dc.subject	Peptides and proteins	en_US
dc.subject	Monomers	en_US
dc.subject	Inhibitors	en_US
dc.title	Synthesis and Structure−Activity Relationships of Linear and Conformationally Constrained Peptide Analogues of CIYKYY as Src Tyrosine Kinase Inhibitors	en_US
dc.type	Article	en_US
Appears in Collections:	Department of Chemistry

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