Furan based Locked Z-Vinylogous γ-Amino Acid Stabilizing Pro-tein α-Turn in Water-Soluble Cyclic α3γ Tetrapeptides

Krishna, Yarkali; Sharma, Shrikant; Ampapathi, R S; Koley, Dipankar

dc.contributor.author	Krishna, Yarkali
dc.contributor.author	Sharma, Shrikant
dc.contributor.author	Ampapathi, R S
dc.contributor.author	Koley, Dipankar
dc.date.accessioned	2014-08-11T07:14:48Z
dc.date.available	2014-08-11T07:14:48Z
dc.date.issued	2014
dc.identifier.citation	Organic Letters, 2014, 16(8), 2084-7	en
dc.identifier.uri	http://hdl.handle.net/123456789/1351
dc.description.abstract	Described here is the design, synthesis and conformational analysis of cyclic tetrapeptides (CTPs) with α3γ architecture containing a furan based locked Z-vinylogous amino acid (Vaa). This unnatural amino acid locks into a γ-turn that induces type IαRS-turn in the CTPs. Stabilized by a 13-membered intramole-cular H-bond these CTPs show robust conformation in water and aprotic solvent irrespective of the se-quence of tripeptide consisting of α-amino acids used.	en
dc.format.extent	1192444 bytes
dc.format.mimetype	application/pdf
dc.language.iso	en	en
dc.relation.ispartofseries	CSIR-CDRI Communication No. 8641	en
dc.subject	Z-Vinylogous	en
dc.subject	γ-Amino Acid	en
dc.subject	Protein	en
dc.subject	α3γ Tetrapeptides	en
dc.title	Furan based Locked Z-Vinylogous γ-Amino Acid Stabilizing Pro-tein α-Turn in Water-Soluble Cyclic α3γ Tetrapeptides	en
dc.type	Article	en