Dataset Information

The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.

ABSTRACT: Collagen fibrils represent a unique case of protein folding and self-association. We have recently successfully developed triple-helical peptides that can further self-assemble into collagen-mimetic mini-fibrils. The 35?nm axially repeating structure of the mini-fibrils, which is designated the d-period, is highly reminiscent of the well-known 67?nm D-period of native collagens when examined using TEM and atomic force spectroscopy. We postulate that it is the pseudo-identical repeating sequence units in the primary structure of the designed peptides that give rise to the d-period of the quaternary structure of the mini-fibrils. In this work, we characterize the self-assembly of two additional designed peptides: peptide Col877 and peptide Col108rr. The triple-helix domain of Col877 consists of three pseudo-identical amino acid sequence units arranged in tandem, whereas that of Col108rr consists of three sequence units identical in amino acid composition but different in sequence. Both peptides form stable collagen triple helices, but only triple helices Col877 self-associate laterally under fibril forming conditions to form mini-fibrils having the predicted d-period. The Co108rr triple helices, however, only form nonspecific aggregates having no identifiable structural features. These results further accentuate the critical involvement of the repeating sequence units in the self-assembly of collagen mini-fibrils; the actual amino acid sequence of each unit has only secondary effects. Collagen is essential for tissue development and function. This novel approach to creating collagen-mimetic fibrils can potentially impact fundamental research and have a wide range of biomedical and industrial applications.

SUBMITTER: Chen F

PROVIDER: S-EPMC6699095 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.

Chen Fangfang F Strawn Rebecca R Xu Yujia Y

Protein science : a publication of the Protein Society 20190901 9

Collagen fibrils represent a unique case of protein folding and self-association. We have recently successfully developed triple-helical peptides that can further self-assemble into collagen-mimetic mini-fibrils. The 35 nm axially repeating structure of the mini-fibrils, which is designated the d-period, is highly reminiscent of the well-known 67 nm D-period of native collagens when examined using TEM and atomic force spectroscopy. We postulate that it is the pseudo-identical repeating sequence ...[more]

PMID: 31299125

Similar Datasets

Project description:The ability to influence the direction of polymerization of a self-assembling biomolecular system has the potential to generate materials with extremely high anisotropy. In biological systems where highly-oriented cellular populations give rise to aligned and often load-bearing tissue such organized molecular scaffolds could aid in the contact guidance of cells for engineered tissue constructs (e.g. cornea and tendon). In this investigation we examine the detailed dynamics of pepsin-extracted type I bovine collagen assembly on a glass surface under the influence of flow between two plates. Differential Interference Contrast (DIC) imaging (60x-1.4NA) with focal plane stabilization was used to resolve and track the growth of collagen aggregates on borosilicate glass for 4 different shear rates (500, 80, 20, and 9s(-1)). The detailed morphology of the collagen fibrils/aggregates was examined using Quick Freeze Deep Etch (QFDE) electron microscopy. Nucleation of fibrils on the glass was observed to occur rapidly (approximately 2 min) followed by continued growth of the fibrils. The growth rates were dependent on flow in a complex manner with the highest rate of axial growth (0.1 micro/s) occurring at a shear rate of 9s(-1). The lowest growth rate occurred at the highest shear. Fibrils were observed to both branch and join during the experiments. The best alignment of fibrils was observed at intermediate shear rates of 20 and 80s(-1). However, the investigation revealed that fibril directional growth was not stable. At high shear rates, fibrils would often turn downstream forming what we term "hooks" which are likely the combined result of monomer interaction with the initial collagen layer or "mat" and the high shear rate. Further, QFDE examination of fibril morphology demonstrated that the assembled fibrillar structure did not possess native D-periodicity. Instead, fibrils comprised a collection of generally aligned, monomers which were self-assembled to form a fibril-like aggregate. In conclusion, though constant shear-rate clearly influences collagen fibrillar alignment, the formation of highly-organized collagenous arrays of native-like D-banded fibrils remains a challenge. Modulation of shear in combination with surface energy patterning to produce a highly-aligned initial mat may provide significant improvement of both the fibril morphology and alignment.

Dataset Information

The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.

Publications

The predominant roles of the sequence periodicity in the self-assembly of collagen-mimetic mini-fibrils.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets