1279034-78-4Relevant articles and documents
Spiegelmeric 4R/S-hydroxy/amino-L/D-prolyl collagen peptides: conformation and morphology of self-assembled structures
Ganesh, Krishna N,More, Shahaji H
, (2020/03/11)
The primary structure of collagen, the major protein in connective tissue of mammals, comprises of repeating triads [(LPro-LHyp-Gly)n, P1, LHyp being 4R-hydroxy-lProline)] in a single strand that adopts left-handed polyproline II type helix. Three such single stranded helices wind around each another and held together by interchain H-bonds to form right-handed triple helix. This manuscript reports on collagen derived from its mirror image triad [(DPro-DHyp-Gly)n, P2, DHyp being 4S-hydroxy-DProline) and its 4-amino analogue (DPro-DAmp-Gly)n P4, DAmp being 4S-amino-DProline that form corresponding spiegelmeric triplexes. The amino L-collagen peptide (LPro-LAmp-Gly)n P3 and its D-analogue P4 show higher thermal stabilities compared to 4-hydroxy-lProline collagen peptides P1 and P2. The enantiomeric peptide pairs show mirror image CD profiles and identical thermal stability, with ionizable 4-amino group in P3 and P4 imparting pH dependent triplex stability. Upon cold mixing of the L- and D-collagen peptides, different morphological nanostructures arise from inter triplex peptide association. When the peptides are hot mixed (annealed), the inter peptide association occurs via interaction of single stranded peptide chains of opposite handedness leading to networked gel formation in P1 and P2, while the charged peptides P3 and P4 show more ordered nanofibers, different from the enantiomerically pure peptides. The nanocomposites of such chiral hybrid peptides may have not only interesting physicomorphology, but also biological properties that need exploration.
Site-directed spin labeling of a collagen mimetic peptide
Jiang, Jianbing,Yang, Longfei,Jin, Qiaoying,Ma, Wude,Moroder, Luis,Dong, Shouliang
supporting information, p. 17679 - 17682 (2014/01/17)
At every turn: Electron paramagnetic resonance spectroscopy was used to investigate the dynamics of triple helix folding/unfolding of host-guest collagen mimetic peptide with a spin-labeled central triplet in Ac-(Gly-Pro-Hyp)7-Gly-Gly-NH2 (see figure). Copyright
Synthesis of alanine and proline amino acids with amino or guanidinium substitution on the side chain
Zhang, Zhenyu,Aerschot, Arthur Van,Hendrix, Chris,Busson, Roger,David, Frank,Sandra, Pat,Herdewijn, Piet
, p. 2513 - 2522 (2007/10/03)
Competitive binding of peptides containing basic amino acids to disrupt or prevent the Tat-TAR interaction could result in diminished transcription as well as translation and hence constitutes an alternative way of controlling HIV replication. Therefore, we synthesized guanidinium and amino containing amino acids, based on a proline or an alanine scaffold. The introduction of the guanidinium moiety was best accomplished using 1H- pyrazole-1-carboxamidine hydrochloride, with Pmc used for its protection. The absence of racemization, maintained throughout the whole synthesis, was confirmed by chiral purity determination. These building blocks were smoothly incorporated into oligopeptides, which proved their suitability for use in a combinatorial approach for selecting TAR binding ligands. (C) 2000 Elsevier Science Ltd.