Self-assembly of <scp>l</scp>-phenylalanine amino acid: electrostatic induced hindrance of fibril formation

Tomar, Deepak; Chaudhary, Shilpi; Jena, Kailash C.

doi:10.1039/c9ra00268e

Cited by 44 publications

(50 citation statements)

References 76 publications

(120 reference statements)

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“…The clear positive signal observed at 222 nm, also observed in previous studies of L-phenylalanine derivatives, was assigned to π-π* transitions resulting from aromatic stacking of the phenylalanine residues. 69 Hence, the self-organization into supramolecular structures of MAm-GFF was attributed to aromatic stacking interactions between FF moieties. In addition, recent experimental and theoretical studies suggested that the self-assembled nanostructures formed from FF-containing molecules are also stabilized via H bonding (FF-FF, FF-solvent) and other weak forces such as hydrophobic, electrostatic and Van der Waals interactions between non-polar moieties.…”

Section: Methacrylamide-functionalized Peptide Monomer Mam-gffmentioning

confidence: 99%

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly

et al. 2020

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Self-assembling peptides (SAP) have been extensively studied for their ability to form nanoscale ordered structures driven by non-covalent molecular interactions. Meanwhile, polymerization-induced self-assembly (PISA) has been exploited as a facile and efficient way to produce various amphiphilic block copolymer nano-objects, whose self-assembly was governed predominantly by the interactions of the different blocks with the polymerization medium. In this work, we combined PISA with SAP to prepare novel peptide-polymer hybrid nano-objects, thus harnessing the advantages of PISA and the self-assembling driving force of SAP. A tripeptide methacrylamide derivative (MAm-Gly-Phe-Phe-NH2, denoted MAm-GFF where MAm means methacrylamide) was copolymerized with glycerol monomethacrylate (GMA) to produce P(GMA65-stat-(MAm-GFF)7) macro-chain transfer agent (macro-CTA) by Reversible addition-fragmentation chain transfer (RAFT) polymerization in DMF.This peptide-based macro-CTA was then successfully chain-extended with poly(2-hydroxypropyl methacrylate) (PHPMA) by aqueous dispersion PISA, forming P(GMA65-stat-(MAm-GFF)7)-b-PHPMA28 self-assembled objects. Fibrous structures were observed by TEM and Cryo-TEM in agreement with DDLS, SLS and SAXS experiments that also revealed long anisotropic morphologies. Such structures have not been reported previously for PISA-prepared nano-objects. This confirms the decisive influence of the GFF SAP on the self-assembly. In addition, annealing the PISA suspension at different temperatures led to a significant size decrease of the self-assembled objects and to a morphological transition caused by the thermo-sensitivity of both the core-forming PHPMA block and the stabilizing P(GMAstat-(MAm-GFF)) block.

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Section: Methacrylamide-functionalized Peptide Monomer Mam-gffmentioning

confidence: 99%

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly

et al. 2020

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“…Not surprisingly, later studies demonstrated the influence of the charged state of Phe ends on the morphology of the aggregates. In particular, in its zwitterionic state, Phe self-assembles into nanostructures with a fibrillary morphology, while in its cationic and anionic state, its aggregates are dominated by a flake morphology ( Tomar et al, 2019 ). Moreover, several studies were also oriented to investigate different aggregation properties and kinetics of L and D -Phe.…”

Section: Going Small: Oligopeptide-based Cross-β Assemblies For Biomamentioning

confidence: 99%

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information

Balasco

Diaferia

Morelli

et al. 2021

Front. Bioeng. Biotechnol.

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The discovery that the polypeptide chain has a remarkable and intrinsic propensity to form amyloid-like aggregates endowed with an extraordinary stability is one of the most relevant breakthroughs of the last decades in both protein/peptide chemistry and structural biology. This observation has fundamental implications, as the formation of these assemblies is systematically associated with the insurgence of severe neurodegenerative diseases. Although the ability of proteins to form aggregates rich in cross-β structure has been highlighted by recent studies of structural biology, the determination of the underlying atomic models has required immense efforts and inventiveness. Interestingly, the progressive molecular and structural characterization of these assemblies has opened new perspectives in apparently unrelated fields. Indeed, the self-assembling through the cross-β structure has been exploited to generate innovative biomaterials endowed with promising mechanical and spectroscopic properties. Therefore, this structural motif has become the fil rouge connecting these diversified research areas. In the present review, we report a chronological recapitulation, also performing a survey of the structural content of the Protein Data Bank, of the milestones achieved over the years in the characterization of cross-β assemblies involved in the insurgence of neurodegenerative diseases. A particular emphasis is given to the very recent successful elucidation of amyloid-like aggregates characterized by remarkable molecular and structural complexities. We also review the state of the art of the structural characterization of cross-β based biomaterials by highlighting the benefits of the osmosis of information between these two research areas. Finally, we underline the new promising perspectives that recent successful characterizations of disease-related amyloid-like assemblies can open in the biomaterial field.

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“…44,45 It was observed that FF and its congeners are able to self-organize into a large variety of NSs from nanotubes to nanofibrils, vesicles, and HGs. [46][47][48] The morphological variability of NSs depends on the experimental procedure adopted for their preparation such as the polarity of the solvent, 49 the pH value or temperature, 50 and by chemical modifications of the aromatic homodimer, including the addition/modification of residues in the sequence, and/or modification of peptide termini. 51,52 Recently, several examples of the HGs based on FF peptide 53 and on its analogues 54 have emerged in literature as potential carriers for the delivery of Dox.…”

Section: Ultra-short and Short Peptide-based Hgsmentioning

confidence: 99%

Peptide‐based hydrogels as delivery systems for doxorubicin

Diaferia

Rosa

Accardo

et al. 2021

Journal of Peptide Science

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Hydrogels (HGs) and nanogels (NGs) have been recently identified as innovative supramolecular materials for many applications in biomedical field such as in tissue engineering, optoelectronic, and local delivery of active pharmaceutical ingredients (APIs). Due to their in vivo biocompatibility, synthetic accessibility, low cost, and tunability, peptides have been used as suitable building blocks for preparation of HGs and NGs formulations. Peptide HGs have shown an outstanding potential to deliver small drugs, protein therapeutics, or diagnostic probes, maintaining the efficacy of their loaded molecules, preventing degradation phenomena, and responding to external physicochemical stimuli. In this review, we discuss the possible use of peptidebased HGs and NGs as vehicles for the delivery of the anticancer drug doxorubicin (Dox). This anthracycline is clinically used for leukemia, stomach, lung, ovarian, breast, and bladder cancer therapy. The loading of Dox into supramolecular systems (liposomes, micelles, hydrogels, and nanogels) allows reducing its cardiotoxicity.According to a primary sequence classification of the constituent peptide, doxorubicin-loaded systems are here classified in short and ultra-short peptide-based HGs, RGD, or RADA-peptide-based HGs and peptide-based NGs.

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Self-assembly of l-phenylalanine amino acid: electrostatic induced hindrance of fibril formation

Abstract: Nanostructure morphology originating from the self-assembly of molecules has attracted substantial attention due to its role in toxic amyloid fibril formation and immense potential in the design and fabrication of novel biomaterials.

Cited by 44 publications

References 76 publications

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly

Self-Assembling Peptide—Polymer Nano-Objects via Polymerization-Induced Self-Assembly

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information

Peptide‐based hydrogels as delivery systems for doxorubicin

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