Synthesis and Β‐conformation of Copolypeptides With Alternating Hydrophilic and Hydrophobic Residues

Brack, A.; Caille, Anita

doi:10.1111/j.1399-3011.1978.tb02831.x

Cited by 56 publications

(9 citation statements)

References 22 publications

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“…To satisfy this requirement we profited from the well-documented observation that in aqueous environments, binary alternating sequences of hydrophobic-hydrophilic residues are prone to oligomerize into amphipathic β-structures. In these structures, the hydrophobic residues are buried at the interface of two β-sheets, leaving the hydrophilic residues on the surface [ 28 , 29 ]. In keeping with the theme of a prebiotic fold, we wanted to use the shortest peptides that still guaranteed a high percentage of amyloidogenic peptides in the library.…”

Section: Resultsmentioning

confidence: 99%

Towards Prebiotic Catalytic Amyloids Using High Throughput Screening

et al. 2015

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Enzymes are capable of directing complex stereospecific transformations and of accelerating reaction rates many orders of magnitude. As even the simplest known enzymes comprise thousands of atoms, the question arises as to how such exquisite catalysts evolved. A logical predecessor would be shorter peptides, but they lack the defined structure and size that are apparently necessary for enzyme functions. However, some very short peptides are able to assemble into amyloids, thereby forming a well-defined tertiary structure called the cross-β-sheet, which bestows unique properties upon the peptides. We have hypothesized that amyloids could have been the catalytically active precursor to modern enzymes. To test this hypothesis, we designed an amyloid peptide library that could be screened for catalytic activity. Our approach, amenable to high-throughput methodologies, allowed us to find several peptides and peptide mixtures that form amyloids with esterase activity. These results indicate that amyloids, with their stability in a wide range of conditions and their potential as catalysts with low sequence specificity, would indeed be fitting precursors to modern enzymes. Furthermore, our approach can be efficiently expanded upon in library size, screening conditions, and target activity to yield novel amyloid catalysts with potential applications in aqueous-organic mixtures, at high temperature and in other extreme conditions that could be advantageous for industrial applications.

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Section: Resultsmentioning

confidence: 99%

Towards Prebiotic Catalytic Amyloids Using High Throughput Screening

et al. 2015

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“…These sequences are 36 monomers long and are constructed from only three different monomers: an aromatic, hydrophobic monomer ( N -(2-phenylethyl)glycine, Npe), and two ionic monomers [ N -(2-aminoethyl)glycine (Nae) and N -(2-carboxyethyl)glycine (Nce)]. They are polymers with a periodic two-fold sequence amphiphilicity, a motif that is known to promote β structure in polypeptides . The oppositely charged strands (Nae–Npe) 18 and (Nce–Npe) 18 (Figure A) attract each other through both hydrophobic and electrostatic interactions and form free-floating nanosheets under dilute aqueous conditions.…”

Section: Resultsmentioning

confidence: 99%

Shaken, Not Stirred: Collapsing a Peptoid Monolayer To Produce Free-Floating, Stable Nanosheets

et al. 2011

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Two-dimensional nanomaterials play a critical role in biology (e.g., lipid bilayers) and electronics (e.g., graphene) but are difficult to directly synthesize with a high level of precision. Peptoid nanosheet bilayers are a versatile synthetic platform for constructing multifunctional, precisely ordered two-dimensional nanostructures. Here we show that nanosheet formation occurs through an unusual monolayer intermediate at the air-water interface. Lateral compression of a self-assembled peptoid monolayer beyond a critical collapse pressure results in the irreversible production of nanosheets. An unusual thermodynamic cycle is employed on a preparative scale, where mechanical energy is used to buckle an intermediate monolayer into a more stable nanosheet. Detailed physical studies of the monolayer-compression mechanism revealed a simple preparative technique to produce nanosheets in 95% overall yield by cyclical monolayer compressions in a rotating closed vial. Compression of monolayers into stable, free-floating products may be a general and preparative approach to access 2D nanomaterials.

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“…In view of these findings, the potency of amphiphilic peptides I and I1 to form stable &structures at very short chain-lengths must be attributed to their ability to form a bilayer structure in aqueous medium which is enhanced by a gain in solvation entrophy. Such bilayer structures have already been proposed for amphiphilic polypeptides (21,23).…”

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confidence: 80%

“…conformational properties of alternating hydrophobic-hydrophilic oligopeptides under various conditions. So far, only the conformational properties of alternating hydrophilic-hydrophobic copolypeptides of high molecular weight (SO00 and higher) have been studied (19)(20)(21)(22)(23)(24)(25)(26), but no information about regularly alternating monodispersed oligopeptides is available. For alternating copoly (Leu-Lys) (23,26), copoly (Leu-Om) (25,26) and copoly (Lys-Phe) (20), &structure formation could be observed in the presence of salts or at high pH.…”

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confidence: 99%

Sequence‐dependence of secondary structure formation

Altmann

Flörsheimer

Mutter

1986

International Journal of Peptide and Protein Research

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The conformational behaviour of the monodisperse amphiphilic oligopeptides (L‐Thr‐L‐Val)n (I and II) and (L‐Ser‐L‐Leu)n (III) for n = 1–4 was investigated by CD spectroscopy in TFE, MeOH and water. A conformational transition random‐coil ‐> ß‐structure was observed for both series: the critical chain length for ß‐structure formation turned out to be dependent on solvent and spatial similarity of the amino acid side‐chains. The very short critical chain‐length for the onset of ß‐structure formation for peptides I and II (n = 3) is explained by the formation of bilayer sheets, in which the minimization of hydrophobic contacts between the amphipilic peptide and the hydrophilic solvent represents an important driving force for ß‐structure formation. The use of amphiphilic peptides for the construction of artificial proteins is briefly discussed.

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Synthesis and Β‐conformation of Copolypeptides With Alternating Hydrophilic and Hydrophobic Residues

Cited by 56 publications

References 22 publications

Towards Prebiotic Catalytic Amyloids Using High Throughput Screening

Towards Prebiotic Catalytic Amyloids Using High Throughput Screening

Shaken, Not Stirred: Collapsing a Peptoid Monolayer To Produce Free-Floating, Stable Nanosheets

Sequence‐dependence of secondary structure formation

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