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Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.

ABSTRACT: The development of novel strategies to construct collagen mimetic peptides capable of self-assembling into higher-order structures plays a critical role in the discovery of functional biomaterials. We herein report the construction of a novel type of amphiphile-like peptide conjugating the repetitive triple helical (GPO) _m sequences characteristic of collagen with terminal hydrophilic aspartic acids. The amphiphile-like collagen mimic peptides containing a variable length of (Gly-Pro-Hyp) _m sequences consistently generate well-ordered nanospherical supramolecular structures. The C-terminal aspartic acids have been revealed to play a determinant role in the appropriate self-assembly of amphiphile-like collagen mimic peptides. Their presence is a prerequisite for self-assembly, and their lengths could modulate the morphology of final assemblies. We have demonstrated for the first time that amphiphile-like collagen mimic peptides with terminal aspartic acids may provide a general and convenient strategy to create well-defined nanostructures in addition to amphiphile-like peptides utilizing β-sheet or α-helical coiled-coil motifs. The newly developed assembly strategy together with the ubiquitous natural function of collagen may lead to the generation of novel improved biomaterials.

SUBMITTER: Yao L

PROVIDER: S-EPMC9077330 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.

Yao Linyan L He Manman M Li Dongfang D Tian Jing J Liu Huanxiang H Xiao Jianxi J

RSC advances 20180110 5

The development of novel strategies to construct collagen mimetic peptides capable of self-assembling into higher-order structures plays a critical role in the discovery of functional biomaterials. We herein report the construction of a novel type of amphiphile-like peptide conjugating the repetitive triple helical (GPO) <sub><i>m</i></sub> sequences characteristic of collagen with terminal hydrophilic aspartic acids. The amphiphile-like collagen mimic peptides containing a variable length of (G ...[more]

PMID: 35541475

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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.

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Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.

Publications

Terminal aspartic acids promote the self-assembly of collagen mimic peptides into nanospheres.

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