The pH-dependent assembly of Chaplin E from Streptomyces coelicolor

Dokouhaki, Mina; Hung, Andrew; Day, Li; Gras, Sally L.

doi:10.1016/j.jsb.2017.04.004

Cited by 8 publications

(18 citation statements)

References 68 publications

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“…Chp F and Chp E also differ in their isoelectric point (pI), although they share 56.4% sequence homology [ 5 ]. A low pI of ~4 was predicted for Chp F, while Chp E has a predicted pI of 6.82 [ 5 ], confirmed experimentally as 6.7 ± 0.3 [ 10 ].…”

Section: Introductionmentioning

confidence: 92%

“…A mixture of chaplins extracted from the cell wall of S. coelicolor is known to lower the surface tension of water in a pH-dependent manner [ 7 , 11 ]. At a high pH (e.g., above 11), a mixture of chaplins exhibits a high surface activity compared to that at pH 2 or 7, leading to a greater reduction of surface activity [ 7 ].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Our previous study showed that altering the pH can lead to different secondary structures in Chp E, each with distinct interfacial properties [ 11 ]. At pH 3.0, Chp E was mostly monomeric or present as small oligomers with a random coil structure [ 10 ] capable of forming ordered structures at the interface that lowered the air/water surface tension to 42 ± 2 mN/m [ 11 ]. Increasing the pH to 6.7 (the pI of Chp E) or 10.0 resulted in a change in the net charge and the distribution of charges over the peptide sequence, leading to the self-assembly of Chp E into β-sheet-rich amyloid fibrils [ 10 ], which oriented randomly at the interface [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

“…At pH 3.0, Chp E was mostly monomeric or present as small oligomers with a random coil structure [ 10 ] capable of forming ordered structures at the interface that lowered the air/water surface tension to 42 ± 2 mN/m [ 11 ]. Increasing the pH to 6.7 (the pI of Chp E) or 10.0 resulted in a change in the net charge and the distribution of charges over the peptide sequence, leading to the self-assembly of Chp E into β-sheet-rich amyloid fibrils [ 10 ], which oriented randomly at the interface [ 11 ]. This structural transition was accompanied by a significant reduction in the surface activity of Chp E [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

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Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor

et al. 2017

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Chaplin F (Chp F) is a secreted surface-active peptide involved in the aerial growth of Streptomyces. While Chp E demonstrates a pH-responsive surface activity, the relationship between Chp F structure, function and the effect of solution pH is unknown. Chp F peptides were found to self-assemble into amyloid fibrils at acidic pH (3.0 or the isoelectric point (pI) of 4.2), with ~99% of peptides converted into insoluble fibrils. In contrast, Chp F formed short assemblies containing a mixture of random coil and β-sheet structure at a basic pH of 10.0, where only 40% of the peptides converted to fibrils. The cysteine residues in Chp F did not appear to play a role in fibril assembly. The interfacial properties of Chp F at the air/water interface were altered by the structures adopted at different pH, with Chp F molecules forming a higher surface-active film at pH 10.0 with a lower area per molecule compared to Chp F fibrils at pH 3.0. These data show that the pH responsiveness of Chp F surface activity is the reverse of that observed for Chp E, which could prove useful in potential applications where surface activity is desired over a wide range of solution pH.

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Section: Introductionmentioning

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Structure-Dependent Interfacial Properties of Chaplin F from Streptomyces coelicolor

et al. 2017

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Fibrous Protein Self‐Assembly in Biomimetic Materials

Mason

Shimanovich

2018

Advanced Materials

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Protein self-assembly processes, by which polypeptides interact and independently form multimeric structures, lead to a wide array of different endpoints. Structures formed range from highly ordered molecular crystals to amorphous aggregates. Order arises in the system from a balance between many low-energy processes occurring due to a set of interactions between residues in a chain, between residues in different chains, and between solute and solvent. In Nature, self-assembling protein systems have evolved over millions of years to organize into supramolecular structures, optimized for specific functions, with this propensity determined by the sequence of their constituent amino acids, of which only 20 are encoded in DNA. The structural materials that arise from biological self-assembly can display remarkable mechanical properties, often as a result of hierarchical structure on the nano- and microscales, and much research has been devoted to mimicking and exploiting these properties for a variety of end uses. This work presents a review of a range of studies in which biological functions are effectively reproduced through the design of self-assembling fibrous protein systems.

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