Influence of different tripeptides on the stability of the collagen triple helix. II. An experimental approach with appropriate variations of a trimer model oligotripeptide

Abstract

SynopsisA collagen model peptide comprising three covalently cross-linked chains (Ala-GlyProIg with a stable triple-helix conformation was utilized as the constant part of elongated model peptides of different composition. The tripeptides Gly-Prc-Hyp, Gly-ProAla, Gly-Pro-Pro, Gly-Pro-Ser, Gly-Afa-Hyp, Gly-Phe-Hyp, Gly-Glu-Hyp, Gly-Ma-Lys, and Gly-Pro-Phe were coupled at the N-terminal to the cross-linked peptide. The transition temperatures determined by CD measurements are higher for the peptides containing the Gly-X-Hyp sequences followed by those with the Gly-Prc-Y sequences. In experiments with combinations of two different tripeptides coupled to the constant part of the cross-linked model peptides higher transition temperatures were observed if the sequence of helix-promoting tripeptides was not interrupted.

Perspectives on the synthesis and application of triple-helical, collagen-model peptides

“…Heidemann and co-workers used nitrophenylsulfenyl or Boc as the N"-amino protecting group, which was removed by moderate acidolysis, benzyloxycarbonyl (Cbz) as the Lys "-amino protecting group, which was removed by strong acidolysis, and 4-(2-chloropropionyl )phenylacetic acid as the linker, allowing for peptide-support cleavage by photolysis or saponification.56359 The assembly of these branched triple-helical peptides was evaluated by ninhydrin testing,58,59 and the final products were characterized by amino acid a n a l y s i~.~~,~* Triple-helix -coil transitions were evaluated from CD melting curves at X = 222-224 nm (Table 11) . [57][58][59] In contrast to associated triple-helical peptides, branched triple-helical peptide melts showed …”

Collagen mimetics

“…66,68 Heidemann and Greiche also studied arrangements of the collagen polypeptides by cross-linking (Gly-Ala-Pro) n (n Å 8, 12, 16) to The folding of the peptide into its secondary or tertiary the 1,2,3-propane tricarboxylic acid backbone. 67 structures is the fundamental requirement to induce Fields et al have employed two consecutively the proper biological response or activity.…”

“…66,68 co-workers to study triple helicity. 57,69 8J1C 5589 / 8J1C$$5589 07-01-98 10:39:48 pscia W: Pep Sci functional groups to link three peptide chains (Figure 3).…”

Design and synthesis of heterotrimeric collagen peptides with a built‐in cystine‐knot Models for collagen catabolism by matrix‐metalloproteases

“…To overcome the unfavorable entropy of nucleating the triple helix in synthetic collagen-like peptides and to increase the thermal stability of the super-helix, covalent linkage of the peptide chains to templates such as 1,2,3-propanetricarboxylic acid or the Lys-Lys dipeptide, has been proposed [10][11][12][13]. The Lys-Lys template approach has extensively been exploited in the solid-phase synthesis of homotrimeric collagenous peptides [14] and even of a heterotrimer [15], despite the serious difficulties encountered in the synthesis and purification of such high molecular weight polypeptides.…”