2008
DOI: 10.1016/j.bmcl.2008.10.076
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Synthesis and biological evaluation of homopiperazine derivatives with β-aminoacyl group as dipeptidyl peptidase IV inhibitors

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Cited by 21 publications
(7 citation statements)
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“…Some functionally important residues lining the active site in DPP4 such as Tyr547 and Asn710 [41], which are provided by the propeller domain, are not conserved in DPP7. In spite of the totally different “selectivity” domains, DPP4 and DPP7 still retain functionally conserved residues participating in both the recognition of the N-terminus of the substrate ( i.e.…”
Section: Resultsmentioning
confidence: 99%
“…Some functionally important residues lining the active site in DPP4 such as Tyr547 and Asn710 [41], which are provided by the propeller domain, are not conserved in DPP7. In spite of the totally different “selectivity” domains, DPP4 and DPP7 still retain functionally conserved residues participating in both the recognition of the N-terminus of the substrate ( i.e.…”
Section: Resultsmentioning
confidence: 99%
“…Ninković et al also recently reported that a large number of phenyl-phenyl contacts in proteins had tilt angles above 60 , corresponding to the T-shaped interaction in the aromatic-aromatic interaction study at a tilt angle range from 0 (parallel) to 90 (T-shaped) by using PDB data 32 . With regard to the hydrogen bonding with the Tyr585, Ahn et al showed that a carboxyl substituent on the homopiperazine derivative appeared to interact with the OZ of Tyr585 in the co-crystal structure of DPP-4, and the acid moiety could regulate CYPs activities 33 .…”
Section: Sar Of Anagliptin Derivativesmentioning
confidence: 99%
“…DPP4 and DPP6 have been shown to form dimers in solution 19 27 . The basis of homodimerization has been attributed to a 2190 Å 2 patch on DPP4 that encompasses the β-propeller and C-terminal loops (PDB-code: 3EIO) 35 . Analogous interactions are seen in DPP6 (PDB-code: 1XFD) and now also in our DPP10 structure, which buries 1580 Å 2 .…”
Section: Resultsmentioning
confidence: 99%