Triple helix–coil transition of covalently bridged collagenlike peptides

Abstract

SynopsisThe thermal triple helix-coil transition of covalently bridged collagenlike peptides with repeating sequences of (Ala-Gly-Pro),, n = 5-15, was studied optically. The peptides were soluble in water/acetic acid (99:l) and were found to form triple-helical structures in this solvent system beginning with n = 8. The thermodynamic analysis of the transition equilibrium curves for n = 9-13 yielded the parameters AH: = -7.0 kJ per tripeptide unit, AS:= -23.1 J deg-' mol-' per tripeptide unit for the coil-to-helix transition, and the apparent nucleation parameter CJ E 5 X lo-*. It was suggested through double-jump temperature experiments that the rate-limiting step during refolding is not only influenced by the difficulties of nucleation, but also by cis-trans isomerization of the Gly-Pro peptide bond.

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).…”

“…ble triple helices. 66,67 Heidemann designed a collagen model peptide composed of three covalently cross-linked chains of (Ala-Gly-Pro) 8 and studied…”

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.…”

A synthetic model of collagen structure taken from bovine macrophage scavenger receptor

“…The collagen is usually synthesized from the C-to N-terminus of the n-i-branched peptide. However, although a peptide covalently cross-linked at the Nterminus has also been reported, this peptide contains only Pro, Ala and Gly, which have no functional groups in the side chains [8].…”