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.SDS of cas: 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: 86069-86-5SDS of cas: 86069-86-5).
(S)-1-(((9H-Fluoren-9-yl)methoxy)carbonyl)piperidine-2-carboxylic acid (cas: 86069-86-5) belongs to piperidine derivatives. The piperidine ring can be found not only in more than half of the currently known structures of alkaloids, but also in many natural or synthetic compounds with interesting biological activities. Fluorinated piperidines are also the subject of continued interest in medicinal chemistry, for example in the synthesis of selective dipeptidyl peptidase II (DPP II) inhibitors. Piperidine derivatives are also used in solid-phase peptide synthesis (SPPS) and many degradation reactions.SDS of cas: 86069-86-5
Referemce:
Piperidine – Wikipedia,
Piperidine | C5H11N – PubChem