A structure-activity relationship study elucidating the mechanism of sequence-specific collagen recognition by the chaperone HSP47 was written by Nishikawa, Yoshimi;Takahara, Yoshifumi;Asada, Shinichi;Shigenaga, Akira;Otaka, Akira;Kitagawa, Kouki;Koide, Takaki. And the article was included in Bioorganic & Medicinal Chemistry in 2010.Reference of 86069-86-5 The following contents are mentioned in the article:
Heat-shock protein 47 (HSP47) is a chaperone that facilitates the proper folding of procollagen. Our previous studies showed that the high-affinity HSP47-binding motif in the collagen triple helix is Xaa-(Thr/Pro)-Gly-Xaa-Arg-Gly. In this study, we further investigated structural requirements for the HSP47-binding motif, using synthetic triple-helical collagen-model peptides with systematic amino acid substitutions at either the Thr/Pro (= Yaa-3) or the Arg (= Yaa0) position. Results obtained from in vitro binding assays indicated that HSP47 detects the side-chain structure of Arg at the Yaa0-position, while the Yaa-3 amino acid serves as the secondary recognition site that affects affinity to HSP47. This study involved multiple reactions and reactants, such as (S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5Reference of 86069-86-5).
(S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5) belongs to piperidine derivatives. Piperidine is a saturated organic heteromonocyclic parent, an azacycloalkane, a secondary amine and a member of piperidines. The piperidine and polyhydroxylated indolizidine derivatives have shown to be promising α-glucosidase inhibitors. The former are analogs of DNJ with an improved α-glucosidase inhibitory profile than that of DNJ. Boisson et al.Reference of 86069-86-5
Referemce:
Piperidine – Wikipedia,
Piperidine | C5H11N – PubChem