The Self-assembly of a Mini-fibril with Axial Periodicity from a Designed Collagen-mimetic Triple Helix

Kaur, Parminder; Strawn, Rebecca; Bai, Hanying; Xu, Ke; Ordas, Gabriel; Matsui, Hiroshi; Xu, Yujia

doi:10.1074/jbc.m113.542241

Cited by 19 publications

(63 citation statements)

References 40 publications

(55 reference statements)

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“…The triple helix domain of Col108 was designed to have an explicit, built-in periodicity of 123 residues in its primary structure by placing three pseudo-identical, 123-residue sequence units in tandem. [28] In the fully folded Col108 triple helix, each sequence unit corresponds to a segment of the triple helix 35 nm in length—the size of a d -period. To create the structural features of gaps and overlaps, we included an overhang unit with a size equivalent to 0.3 d (~10 nm) comprised of the N and C-terminal sections of peptide bracketing the three sequence units; specifically, the overhang consists of an N-terminal Cys-knot sequence, a C-terminal nucleation sequence, a C-terminal Cys-knot sequence and a C-terminal foldon domain.…”

Section: Introductionmentioning

confidence: 99%

“…This unit-staggered model is supported by the Observation of an axially repeating structure of exactly 35 nm for the self-assembled Col108 mini-fibrils, consisting of an ~25 nm (0.7 d ) gap region and an ~10 nm (0.3 d ) overlap region. [28] To test the robustness of this design strategy, we have made two new peptides: 2U108 and 1U108 containing, respectively, two and one sequence units. Thus, the 123-residue sequence periodicity is maintained in 2U108 but not in 1U108.…”

Section: Introductionmentioning

confidence: 99%

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To achieve self‐assembled collagen mimetic fibrils using designed peptides

et al. 2018

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It has proven challenging to obtain collagen-mimetic fibrils by protein design. We recently reported the self-assembly of a mini-fibril showing a 35 nm, D-period like, axially repeating structure using the designed triple helix Col108. Peptide Col108 was made by bacterial expression using a synthetic gene; its triple helix domain consists of three pseudo-identical units of amino acid sequence arranged in tandem. It was postulated that the 35 nm d-period of Col108 mini-fibrils originates from the periodicity of the Col108 primary structure. A mutual staggering of one sequence unit of the associating Col108 triple helices can maximize the inter-helical interactions and produce the observed 35 nm d-period. Based on this unit-staggered model, a triple helix consisting of only two sequence units is expected to have the potential to form the same d-periodic mini-fibrils. Indeed, when such a peptide, peptide 2U108, was made it was found to self-assemble into mini-fibrils having the same d-period of 35 nm. In contrast, no d-periodic mini-fibrils were observed for peptide 1U108, which does not have long-range repeating sequences in its primary structure. The findings of the periodic mini-fibrils of Col108 and 2U108 suggest a way forward to create collagen-mimetic fibrils for biomedical and industrial applications.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

To achieve self‐assembled collagen mimetic fibrils using designed peptides

et al. 2018

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“…This is hindered by the requirement for proline hydroxylation, which has proven difficult in E. coli, though expression can be achieved by exploiting folding catalyst over-expression [112] while collagen mimetics of various formats have also been efficiently expressed in E. coli. [113,114] Native collagen is frequently expressed, however, in non-procaryotic expression systems such as yeast, [115] insect [115c] or plant [116] species for purification and utilization.…”

Section: Expression Systems For Recombinant Productsmentioning

confidence: 99%

Adding Functions to Biomaterial Surfaces through Protein Incorporation

et al. 2016

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The concept of biomaterials has evolved from one of inert mechanical supports with a long-term, biologically inactive role in the body into complex matrices that exhibit selective cell binding, promote proliferation and matrix production, and may ultimately become replaced by newly generated tissues in vivo. Functionalization of material surfaces with biomolecules is critical to their ability to evade immunorecognition, interact productively with surrounding tissues and extracellular matrix, and avoid bacterial colonization. Antibody molecules and their derived fragments are commonly immobilized on materials to mediate coating with specific cell types in fields such as stent endothelialization and drug delivery. The incorporation of growth factors into biomaterials has found application in promoting and accelerating bone formation in osteogenerative and related applications. Peptides and extracellular matrix proteins can impart biomolecule- and cell-specificities to materials while antimicrobial peptides have found roles in preventing biofilm formation on devices and implants. In this progress report, we detail developments in the use of diverse proteins and peptides to modify the surfaces of hard biomaterials in vivo and in vitro. Chemical approaches to immobilizing active biomolecules are presented, as well as platform technologies for isolation or generation of natural or synthetic molecules suitable for biomaterial functionalization.

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“…We can conclude from Table 2 that self-assembly at pH 7.0 led to more collagen molecule being assembled and the fibrils at pH 7.0 were thicker, and the fibrils formed at alkaline pH tend to be narrow in diameter, because the pH of collagen solution may be close the isoelectric point (pI) of collagen. At certain concentration, the collagen molecules are connected to be linear molecules for the mutual repulsion of -NH 3+ -, lysine, and arginine on the polypeptide chain and histidine residues [26,27]. But the hydrogen bonding and ionic bonding between collagen molecules were damaged by excessive acid or alkali.…”

Section: Effects Of Ph Values On the Collagen Self-assemblymentioning

confidence: 99%

“…In the meantime, the collagen would be filled with water when pH value is below the isoelectric point of collagen and shows the acid expansion that is positively charged; oppositely, the collagen will be negatively charged and show alkaline expansion [27]. The moisture holding capacity of collagen varies with the pH values of buffer solution [26], which will help to further understand the mechanism of collagen self-assembly and provide the reference for collagen molecules assembly into fibers.…”

Section: Effects Of Ph Values On the Collagen Self-assemblymentioning

confidence: 99%

Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

Song

Wang

Tao

et al. 2017

Journal of Food Quality

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Self-assembly of extracted collagen from swine trotter tendon under different conditions was firstly observed using atomic force microscopy; then the effects of collagen concentration, pH value, and metal ions to the topography of the collagen assembly were analyzed with the height images and section analysis data. Collagen assembly under 0.1 M, 0.2 M, 0.3 M CaCl 2 , and MgCl 2 solutions in different pH values showed significant differences (P < 0.05) in the topographical properties including height, width, and roughness. With the concentration being increased, the width of collagen decreased significantly (P < 0.05). The width of collagen fibers was first increased significantly (P < 0.05) and then decreased with the increasing of pH. The collagen was assembled with network structure on the mica in solution with Ca 2+ ions. However, it had shown uniformed fibrous structure with Mg 2+ ions on the new cleaved mica sheet. In addition, the width of collagen fibrous was 31∼58 nm in solution with Mg 2+ but 21∼50 nm in Ca 2+solution. The self-assembly collagen displayed various potential abilities to construct fibers or membrane on mica surfaces with Ca 2+ ions and Mg 2+ irons. Besides, the result of collagen self-assembly had shown more relations among solution pH value, metal ions, and collagen molecular concentration, which will provide useful information on the control of collagen self-assembly in tissue engineering and food packaging engineering.

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The Self-assembly of a Mini-fibril with Axial Periodicity from a Designed Collagen-mimetic Triple Helix

Cited by 19 publications

References 40 publications

To achieve self‐assembled collagen mimetic fibrils using designed peptides

To achieve self‐assembled collagen mimetic fibrils using designed peptides

Adding Functions to Biomaterial Surfaces through Protein Incorporation

Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

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