The effect of pH on the self-assembly of a collagen derived peptide amphiphile

Dehsorkhi, Ashkan; Castelletto, Valeria; Hamley, Ian W.; Adamčík, Jozef; Mezzenga, Raffaele

doi:10.1039/c3sm51029h

Cited by 58 publications

(66 citation statements)

References 19 publications

(33 reference statements)

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“…31 As shown in Fig. 3b, the peptide motif KLVFF (Aβ [16][17][18][19][20] self-assembled into 2D membranes under the influence of hydrated electrons coming from argon glow discharge. Meanwhile, the metal ions in solution could be simultaneously reduced to MNPs (Au, Pt, Ag and Pd) by these high-energy electrons.…”

Section: Peptide and Noble Mnp Nanohybridsmentioning

confidence: 90%

“…18,34,95,96 For example, due to its effect on migrating and adhering endothelial cells, collagen-mimetic peptide containing sequence RGD is expected to mimicking extracellular matrix (ECM) for a long period of time. 34 In a metal-promoted assembly process, metal-ligand pairs could serve as anchors for the crosslinking of His-tagged biomolecules.…”

Section: Other Applicationsmentioning

confidence: 99%

“…A group led by Mezzenga has so far performed a lot amyloid-related works, including mechanism of amyloid-peptide self-assembly, influence of ion strength, pH, temperature and functionalization of peptide. 18 Recently, several exciting applications based on the self-assembled amyloid-NP nanohybrids, such as shape-memory materials, 101 biosensors, 102 and bone biomineralization, 86 have been reported by the Mezzenga group.…”

Section: Other Applicationsmentioning

confidence: 99%

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Design, fabrication, and biomedical applications of bioinspired peptide–inorganic nanomaterial hybrids

Wang

et al. 2017

J. Mater. Chem. B

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By specifically binding with various inorganic nanomaterials through their functional groups or introducing a special reactivity, the nanostructures and biofunctions of designed peptides are able to be enriched. This review provides a brief discussion on the design, composition and biomedical applications of bioinspired peptide-inorganic nanomaterial hybrids. The attaching mechanism of different peptide-inorganic nanomaterials are discussed from the view of the functional group, nanostructure, and conformational freedom. Particularly, the structures and functions of the obtained hybrids based on different nanomaterials are described in detail. In addition, we highlight some examples of self-assembled peptide-inorganic nanomaterial systems with relevance to biomedical applications including biosensors, cell targeting, bioimaging, biomineralization, biocatalyst, drug delivery and others. We also give a short outlook on the broad prospect of fabrication and applications of peptide-inorganic nanomaterial hybrids.

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Section: Peptide and Noble Mnp Nanohybridsmentioning

confidence: 90%

Section: Other Applicationsmentioning

confidence: 99%

Section: Other Applicationsmentioning

confidence: 99%

See 1 more Smart Citation

Design, fabrication, and biomedical applications of bioinspired peptide–inorganic nanomaterial hybrids

Wang

et al. 2017

J. Mater. Chem. B

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“…The difference of Rms roughness was also significant (P < 0.05) at different pH values. It was demonstrated that the solution of pH values played an important role in influencing the adsorption of anions and cations at the solid-liquid interfaces during collagen selfassembly [21,22]. The molecular structure of collagen is the trimer-of-phase [ 1 (I)] 2 2 (I), which is composed of 1 (I) and 2 (I) chains.…”

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 PA C 16 -KTTKS has been shown to have β-sheet secondary structure and form bilayer-based nanotapes 32 which are stable between the pH range of 3-7 at room temperature. However, pH reduction/increase 64 or increased temperature 65 favours random coil secondary structure, and spherical micelle self-assembly.…”

mentioning

confidence: 99%

Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

2017

Self Cite

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Molecular self-assembly is a multi-disciplinary field of research, with potential chemical and biological applications. One of the main driving forces of self-assembly is molecular amphiphilicity, which can drive formation of complex and stable nanostructures. Self-assembling peptide and peptide conjugates have attracted great attention due to their biocompatibility, biodegradability and biofunctionality. Understanding assembly enables the better design of peptide amphiphiles which may form useful and functional nanostructures. This review covers self-assembly of amphiphilic peptides and peptide mimetic materials, as well as their potential applications. Peptide self-assemblySelf-assembly is defined as the ability of a molecule, without guidance of external factors, to associate through non-covalent interactions to form highly ordered 3-dimensional structures.

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The effect of pH on the self-assembly of a collagen derived peptide amphiphile

Cited by 58 publications

References 19 publications

Design, fabrication, and biomedical applications of bioinspired peptide–inorganic nanomaterial hybrids

Design, fabrication, and biomedical applications of bioinspired peptide–inorganic nanomaterial hybrids

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

Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials

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