Tryptophan-PNA gc Conjugates Self-Assemble to Form Fibers

Mosseri, Andrea; Sancho‐Albero, María; Mercurio, Flavia Anna; Leone, Marilisa; Cola, Luisa De; Romanelli, Alessandra

doi:10.1021/acs.bioconjchem.3c00200

Cited by 3 publications

(2 citation statements)

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“…This structure represented the dimeric arrangement of the WW dipeptide units. The selected dimeric structure was then utilized to develop WWgc conjugates (g and c stand for guanine and cytosine PNA monomeric units), which are essential for the formation of WWgc fibers [45]. Overall, the study demonstrated how molecular docking techniques could be employed to investigate the self-aggregation of amino acid units and to model the formation of higher-order structures such as WWgc fibers.…”

Section: Self-assembly and Biological Properties Of The Non-natural A...mentioning

confidence: 99%

“…This study demonstrates the utility of molecular docking simulations in elucidating the self-assembly mechanism of peptide-based materials, providing valuable insights into their structural organization and potential applications in supramolecular gelation. In the paper by Mosseri et al, molecular docking was utilized to construct a model of a WWgc fiber starting from a WW dipeptide unit [45]. The dipeptide unit was used as both a receptor and a ligand in the Haddock software [46][47][48][49][50] to predict its dimeric form through molecular docking techniques.…”

Section: Self-assembly and Biological Properties Of The Non-natural A...mentioning

confidence: 99%

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BSA Binding and Aggregate Formation of a Synthetic Amino Acid with Potential for Promoting Fibroblast Proliferation: An In Silico, CD Spectroscopic, DLS, and Cellular Study

Simonyan,

Palumbo,

Petrosyan

et al. 2024

Biomolecules

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This study presents the chemical synthesis, purification, and characterization of a novel non-natural synthetic amino acid. The compound was synthesized in solution, purified, and characterized using NMR spectroscopy, polarimetry, and melting point determination. Dynamic Light Scattering (DLS) analysis demonstrated its ability to form aggregates with an average size of 391 nm, extending to the low micrometric size range. Furthermore, cellular biological assays revealed its ability to enhance fibroblast cell growth, highlighting its potential for tissue regenerative applications. Circular dichroism (CD) spectroscopy showed the ability of the synthetic amino acid to bind serum albumins (using bovine serum albumin (BSA) as a model), and CD deconvolution provided insights into the changes in the secondary structures of BSA upon interaction with the amino acid ligand. Additionally, molecular docking using HDOCK software elucidated the most likely binding mode of the ligand inside the BSA structure. We also performed in silico oligomerization of the synthetic compound in order to obtain a model of aggregate to investigate computationally. In more detail, the dimer formation achieved by molecular self-docking showed two distinct poses, corresponding to the lowest and comparable energies, with one pose exhibiting a quasi-coplanar arrangement characterized by a close alignment of two aromatic rings from the synthetic amino acids within the dimer, suggesting the presence of π-π stacking interactions. In contrast, the second pose displayed a non-coplanar configuration, with the aromatic rings oriented in a staggered arrangement, indicating distinct modes of interaction. Both poses were further utilized in the self-docking procedure. Notably, iterative molecular docking of amino acid structures resulted in the formation of higher-order aggregates, with a model of a 512-mer aggregate obtained through self-docking procedures. This model of aggregate presented a cavity capable of hosting therapeutic cargoes and biomolecules, rendering it a potential scaffold for cell adhesion and growth in tissue regenerative applications. Overall, our findings highlight the potential of this synthetic amino acid for tissue regenerative therapeutics and provide valuable insights into its molecular interactions and aggregation behavior.

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Section: Self-assembly and Biological Properties Of The Non-natural A...mentioning

confidence: 99%

Section: Self-assembly and Biological Properties Of The Non-natural A...mentioning

confidence: 99%

BSA Binding and Aggregate Formation of a Synthetic Amino Acid with Potential for Promoting Fibroblast Proliferation: An In Silico, CD Spectroscopic, DLS, and Cellular Study

Simonyan,

Palumbo,

Petrosyan

et al. 2024

Biomolecules

View full text Add to dashboard Cite

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Hybrid peptide‐PNA monomers as building blocks for the fabrication of supramolecular aggregates

Cimmino,

Diaferia,

Rosa

et al. 2024

Journal of Peptide Science

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Advantages like biocompatibility, biodegradability and tunability allowed the exploitation of peptides and peptidomimetics as versatile therapeutic or diagnostic agents. Because of their selectivity towards transmembrane receptors or cell membranes, peptides have also been identified as suitable molecules able to deliver in vivo macromolecules, proteins or nucleic acids. However, after the identification of the homodimer diphenylalanine (FF) as an aggregative motif inside the Aβ1–42 polypeptide, short and ultrashort peptides have been studied as building blocks for the fabrication of supramolecular, ordered nanostructures for applications in biotechnological, biomedical and industrial fields. In this perspective, many hybrid molecules that combine FF with other chemical entities have been synthesized and characterized. Two novel hybrid derivatives (tFaF and cFgF), in which the FF homodimer is alternated with the peptide‐nucleic acid (PNA) heterodimer “g‐c” (guanine‐cytosine) or “a‐t” (adenine‐thymine) and their dimeric forms (tFaF)2 and (cFgF)2 were synthesized. The structural characterization performed by circular dichroism (CD), Fourier transform infrared (FTIR) and fluorescence spectroscopies highlighted the capability of all the FF‐PNA derivatives to self‐assemble into β‐sheet structures. As a consequence of this supramolecular organization, the resulting aggregates also exhibit optoelectronic properties already reported for other similar nanostructures. This photoemissive behavior is promising for their potential applications in bioimaging.

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Au(I) complexes installed on a self‐assembled peptide efficiently catalyze intramolecular cyclization reactions

Pirovano,

Brini,

Brambilla

et al. 2024

Journal of Peptide Science

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Self‐assembled peptides are used for diverse applications in the biomedical and technological fields. The morphology and function of the assembled systems are dictated by the peptide sequence and length. In this work, a supramolecular catalyst was obtained upon self‐assembly of the diphenylalanine peptide conjugated to a triphenylphosphine Au(I) complex in acetonitrile. The assembled molecules were characterized by spectroscopic techniques and by scanning electron microscopy. The activity of the catalyst was tested on two substrates in cyclization reactions. The morphology and the dimensions of the assembled systems vary depending on the presence of a carboxyl versus an amide C‐terminal end. The catalyst efficiently promotes intramolecular cyclization reactions. Results obtained encourage the use of self‐assembled peptides for the obtainment of new and efficient catalysts.

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Tryptophan-PNA gc Conjugates Self-Assemble to Form Fibers

Cited by 3 publications

References 50 publications

BSA Binding and Aggregate Formation of a Synthetic Amino Acid with Potential for Promoting Fibroblast Proliferation: An In Silico, CD Spectroscopic, DLS, and Cellular Study

BSA Binding and Aggregate Formation of a Synthetic Amino Acid with Potential for Promoting Fibroblast Proliferation: An In Silico, CD Spectroscopic, DLS, and Cellular Study

Hybrid peptide‐PNA monomers as building blocks for the fabrication of supramolecular aggregates

Au(I) complexes installed on a self‐assembled peptide efficiently catalyze intramolecular cyclization reactions

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