Oligoprolines as Scaffolds for the Formation of Silver Nanoparticles in Defined Sizes: Correlating Molecular and Nanoscopic Dimensions

Upert, Grégory; Bouillère, Francelin; Wennemers, Helma

doi:10.1002/anie.201107183

Cited by 61 publications

(52 citation statements)

References 59 publications

(22 reference statements)

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“…Oligoprolines, which are amongst the most rigid peptides, have become increasingly popular in recent years as “molecular rulers” and “molecular scaffolds” 1. They have been used for energy transfer,2–8 distance measurements in biomolecules,9, 10 tumor targeting,11, 12 electron‐transfer studies,13, 14 the development of protein– protein interaction inhibitors,15 hierarchical supramolecular assemblies,16 and for the size‐controlled formation of metal nanoparticles 17. Thus, detailed knowledge of the dimensions and conformational rigidity of oligoprolines is highly sought after.…”

Section: Introductionmentioning

confidence: 99%

Shape Persistence of Polyproline II Helical Oligoprolines

Garbuio

Lewandowski

Wilhelm

et al. 2015

Chemistry A European J

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Oligoprolines are commonly used as molecular scaffolds. Past studies on the persistence length of their secondary structure, the polyproline II (PPII) helix, and on the fraction of backbone cis amide bonds have provided conflicting results. We resolved this debate by studying a series of spin-labeled proline octadecamers with EPR spectroscopy. Distance distributions between an N-terminal Gd(III) -DOTA (DOTA=1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid) label and a nitroxide label at one of five evenly spaced backbone sites allowed us to discriminate between the flexibility of the PPII helix and the cis amide contributions. An upper limit of 2 % cis amide bonds per residue was found in a 7:3 (v/v) water/glycerol mixture, whereas cis amides were not observed in trifluoroethanol. Extrapolation of Monte Carlo models from the glass transition to ambient temperature predicts a persistence length of ≈3-3.5 nm in both solvents. The method is generally applicable to any type of oligomer for which the persistence length is of interest.

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Section: Introductionmentioning

confidence: 99%

Shape Persistence of Polyproline II Helical Oligoprolines

Garbuio

Lewandowski

Wilhelm

et al. 2015

Chemistry A European J

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“…Thes tructures established by NMR showed that all the side chains of Agl-Phe building blocks were periodically distributed in defined spatial arrangements on both sides of the ribbon-like structure (Figure 1). [14] In the case of Agl-AA x oligomers,al arge diversity of functional groups could be easily introduced thanks to the initial Met/AA x peptide sequence, thus providing al arge variety of structured oligomers without further post-functionalization. [14] In the case of Agl-AA x oligomers,al arge diversity of functional groups could be easily introduced thanks to the initial Met/AA x peptide sequence, thus providing al arge variety of structured oligomers without further post-functionalization.…”

Section: Angewandte Zuschriftenmentioning

confidence: 99%

Turning Peptide Sequences into Ribbon Foldamers by a Straightforward Multicyclization Reaction

et al. 2015

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The conformational control of molecular scaffolds allows the displayo ff unctional groups in defined spatial arrangement. This is of considerable interest for developing fundamental and applied systems in both the fields of biology and material sciences.P eptides affordalarge diversity of functional groups,a nd peptide synthetic routes are very attractive and accessible.H owever,m ost short peptides do not possess well-defined secondary structures.H erein, we developed as imple strategy for converting peptide sequences into structured g-lactam-containing oligomers while keeping the amino acids side chain diversity.Weshowed the propensity of these molecules to adopt ribbon-likes econdary structures. The periodic distribution of the functional groups on both sides of the ribbon plane is encoded by the initial peptide sequence.Since the pioneering works of Gellman [1] and Seebach, [2]

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“…Peptides are valuable for the formation of biocompatible noble‐metal nanoparticles . We therefore envisioned that peptidic ligands would also enable the preparation of stable PtNPs in aqueous solution and, moreover, could be tailored to allow for their uptake into liver cancer cells and subsequent oxidation of Pt 0 to Pt II .…”

Section: Figurementioning

confidence: 99%

Peptide‐Coated Platinum Nanoparticles with Selective Toxicity against Liver Cancer Cells

et al. 2019

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Peptide‐stabilized platinum nanoparticles (PtNPs) were developed that have significantly greater toxicity against hepatic cancer cells (HepG2) than against other cancer cells and non‐cancerous liver cells. The peptide H‐Lys‐Pro‐Gly‐dLys‐NH2 was identified by a combinatorial screening and further optimized to enable the formation of water‐soluble, monodisperse PtNPs with average diameters of 2.5 nm that are stable for years. In comparison to cisplatin, the peptide‐coated PtNPs are not only more toxic against hepatic cancer cells but have a significantly higher tumor cell selectivity. Cell viability and uptake studies revealed that high cellular uptake and an oxidative environment are key for the selective cytotoxicity of the peptide‐coated PtNPs.

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Oligoprolines as Scaffolds for the Formation of Silver Nanoparticles in Defined Sizes: Correlating Molecular and Nanoscopic Dimensions

Cited by 61 publications

References 59 publications

Shape Persistence of Polyproline II Helical Oligoprolines

Shape Persistence of Polyproline II Helical Oligoprolines

Turning Peptide Sequences into Ribbon Foldamers by a Straightforward Multicyclization Reaction

Peptide‐Coated Platinum Nanoparticles with Selective Toxicity against Liver Cancer Cells

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