Synthesis, Self-Assembly, and Biological Activities of Pyrimidine-Based Cationic Amphiphiles

Diketopiperazine Gels: New Horizons from the Self-Assembly of Cyclic Dipeptides

Molecules ◽

10.3390/molecules26113376 ◽

2021 ◽

Vol 26 (11) ◽

pp. 3376

Author(s):

Marco Scarel ◽

Silvia Marchesan

Keyword(s):

Drug Discovery ◽

Enzymatic Hydrolysis ◽

Self Assembly ◽

Biological Activities ◽

Functional Materials ◽

The Self ◽

Cyclic Dipeptides ◽

New Horizons ◽

Concise Review

Cyclodipeptides (CDPs) or 2,5-diketopiperazines (DKPs) can exert a variety of biological activities and display pronounced resistance against enzymatic hydrolysis as well as a propensity towards self-assembly into gels, relative to the linear-dipeptide counterparts. They have attracted great interest in a variety of fields spanning from functional materials to drug discovery. This concise review will analyze the latest advancements in their synthesis, self-assembly into gels, and their more innovative applications.

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A conformational tweak for enhanced cellular internalization, photobleaching resistance and prolonged imaging efficacy

Chemical Communications ◽

10.1039/d0cc05557c ◽

2020 ◽

Vol 56 (94) ◽

pp. 14861-14864

Author(s):

Niranjan Meher ◽

Anil Parsram Bidkar ◽

Debasish Barman ◽

Siddhartha Sankar Ghosh ◽

Parameswar Krishnan Iyer

Keyword(s):

Self Assembly ◽

Biological Activities ◽

Cellular Internalization ◽

Molecular Systems ◽

Simple Strategy ◽

Fine Tune

A simple strategy of conformational manipulation has been unveiled to fine-tune the photophysical and supramolecular self-assembly properties of small molecular systems, which subsequently regulates their biological activities.

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Heterometallic BODIPY-Based Molecular Squares Obtained by Self-Assembly: Synthesis and Biological Activities

ACS Omega ◽

10.1021/acsomega.9b01328 ◽

2019 ◽

Vol 4 (8) ◽

pp. 13200-13208 ◽

Cited By ~ 3

Author(s):

Gajendra Gupta ◽

Yeji You ◽

Rizky Hadiputra ◽

Jaehoon Jung ◽

Dong-Ku Kang ◽

...

Keyword(s):

Self Assembly ◽

Biological Activities ◽

Molecular Squares

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Aβ(M1–40) and Wild-Type Aβ40 Self-Assemble into Oligomers with Distinct Quaternary Structures

Molecules ◽

10.3390/molecules24122242 ◽

2019 ◽

Vol 24 (12) ◽

pp. 2242 ◽

Cited By ~ 1

Author(s):

Jacob L. Bouchard ◽

Taylor C. Davey ◽

Todd M. Doran

Keyword(s):

Self Assembly ◽

Quaternary Structure ◽

Biological Activities ◽

Amyloid Β ◽

Long Term Potentiation ◽

Wild Type ◽

Molecular Weights ◽

Term Potentiation ◽

Quaternary Structures

Amyloid-β oligomers (AβOs) self-assemble into polymorphic species with diverse biological activities that are implicated causally to Alzheimer’s disease (AD). Synaptotoxicity of AβO species is dependent on their quaternary structure, however, low-abundance and environmental sensitivity of AβOs in vivo have impeded a thorough assessment of structure–function relationships. We developed a simple biochemical assay to quantify the relative abundance and morphology of cross-linked AβOs. We compared oligomers derived from synthetic Aβ40 (wild-type (WT) Aβ40) and a recombinant source, called Aβ(M1–40). Both peptides assemble into oligomers with common sizes and morphology, however, the predominant quaternary structures of Aβ(M1–40) oligomeric states were more diverse in terms of dispersity and morphology. We identified self-assembly conditions that stabilize high-molecular weight oligomers of Aβ(M1–40) with apparent molecular weights greater than 36 kDa. Given that mixtures of AβOs derived from both peptides have been shown to be potent neurotoxins that disrupt long-term potentiation, we anticipate that the diverse quaternary structures reported for Aβ(M1–40) oligomers using the assays reported here will facilitate research efforts aimed at isolating and identifying common toxic species that contribute to synaptic dysfunction.

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The Development and Lifetime Stability Improvement of Guanosine-Based Supramolecular Hydrogels through Optimized Structure

BioMed Research International ◽

10.1155/2019/6258248 ◽

2019 ◽

Vol 2019 ◽

pp. 1-18 ◽

Cited By ~ 5

Author(s):

Miao Chen ◽

Weimin Lin ◽

Le Hong ◽

Ning Ji ◽

Hang Zhao

Keyword(s):

Self Assembly ◽

Molecular Level ◽

Biological Activities ◽

Research Progress ◽

Self Healing ◽

Base Modification ◽

Structural Framework ◽

Important Building Block ◽

Targeted Release ◽

Excess Cations

Guanosine is an important building block for supramolecular gels owing to the unique self-assembly property that results from the unique hydrogen bond acceptors and donor groups. Guanosine-derived supramolecular hydrogels have promise in the fields of drug delivery, targeted release, tissue engineering applications,etc.However, the property of poor longevity and the need for excess cations hinder the widespread applications of guanosine hydrogels. Although guanosine-derived supramolecular hydrogels have been reviewed previously by Dash et al., the structural framework of this review is different, as the modification of guanosine is described at the molecular level. In this review, we summarize the development and lifetime stability improvement of guanosine-based supramolecular hydrogels through optimized structure and elaborate on three aspects: sugar modification, base modification, and binary gels. Additionally, we introduce the concept and recent research progress of self-healing gels, providing inspiration for the development of guanosine-derived supramolecular hydrogels with longer lifespans, unique physicochemical properties, and biological activities.

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Hydrogelation Through Self-Assembly of Fmoc-Peptide Functionalized Cationic Amphiphiles: Potent Antibacterial Agent

The Journal of Physical Chemistry B ◽

10.1021/jp909520w ◽

2010 ◽

Vol 114 (13) ◽

pp. 4407-4415 ◽

Cited By ~ 108

Author(s):

Sisir Debnath ◽

Anshupriya Shome ◽

Dibyendu Das ◽

Prasanta Kumar Das

Keyword(s):

Self Assembly ◽

Antibacterial Agent ◽

Cationic Amphiphiles

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Enzyme mediated synthesis of hybrid polyedric gold nanoparticles

Scientific Reports ◽

10.1038/s41598-021-81751-1 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Célia Arib ◽

Jolanda Spadavecchia ◽

Marc Lamy de la Chapelle

Keyword(s):

Gold Nanoparticles ◽

Self Assembly ◽

Manganese Superoxide Dismutase ◽

Protein Complexes ◽

Biological Activities ◽

Production Method ◽

Cellular Mechanisms ◽

Manganese Superoxide ◽

Gold Salts ◽

One Step

AbstractLarge protein complexes carry out some of the most complex activities in biology1,2. Such structures are often assembled spontaneously through the process of self-assembly and have characteristic chemical or biological assets in the cellular mechanisms3. Gold-based nanomaterials have attracted much attention in many areas of chemistry, physics and biosciences because of their size- and shape-dependent optic, electric, and catalytic properties. Here we report for the first time a one step synthesis in which Manganese Superoxide Dismutase protein plays a key role in the reduction of gold salts via the use of a Good's buffer (HEPES) to produce gold nanoparticles, compared to other proteins as catalase (CAT) and bovine serum albumin (BSA).We prove that this effect is directly related with the biological activities of the proteins that have an effect on the gold reduction mechanisms. Such synthesis route also induces the integration of proteins directly in the AuNPs that are intrinsically safe by design using a one-step production method. This is an important finding that will have uses in various applications, particularly in the green synthesis of novel nanomaterials.

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The Human LL-37(17-29) Antimicrobial Peptide Reveals a Functional Supramolecular Nanostructure

10.1101/2020.02.04.933432 ◽

2020 ◽

Cited By ~ 2

Author(s):

Yizhaq Engelberg ◽

Meytal Landau

Keyword(s):

Lipid Bilayers ◽

Self Assembly ◽

Amyloid Fibrils ◽

Biological Activities ◽

Building Blocks ◽

Bacterial Cells ◽

Bacterial Membranes ◽

Self Assembling ◽

Wide Ribbon ◽

Wide Range

Protein fibrils that perform biological activities present attractive biomaterials. Here we demonstrate, by crystal structures, the self-assembly of the antibacterial human LL-37 active core (residues 17-29) into a stable structure of densely packed helices. The surface of the fibril encompasses alternating hydrophobic and positively charged zigzagged belts, which likely underlie interactions with and subsequent disruption of negatively charged lipid bilayers, such as bacterial membranes. LL-3717-29 correspondingly formed wide, ribbon-like, thermostable fibrils in solution, which co-localized with bacterial cells, and structure-guided mutagenesis analyses supported the role of self-assembly in antibacterial activity. LL-3717-29 resembled, in sequence and in the ability to form amphipathic helical fibrils, the bacterial cytotoxic PSMα3 peptide that assembles into cross-α amyloid fibrils. This suggests helical, self-assembling, basic building blocks across kingdoms of life and point to potential structural mimicry mechanisms. The findings offer a scaffold for functional and durable nanostructures for a wide range of medical and technological applications.

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Native oligomerization determines the mode of action and biological activities of human cathelicidin LL-37

Biochemical Journal ◽

10.1042/bj20131048 ◽

2013 ◽

Vol 457 (2) ◽

pp. 263-275 ◽

Cited By ~ 42

Author(s):

Daniela Xhindoli ◽

Sabrina Pacor ◽

Filomena Guida ◽

Nikolinka Antcheva ◽

Alessandro Tossi

Keyword(s):

Self Assembly ◽

Mode Of Action ◽

Biological Activities ◽

Biological Membranes ◽

Innate Immune ◽

Cross Linking ◽

Covalent Dimerization

Covalent dimerization and photochemical cross-linking were used to study self-assembly in the multifunctional innate immune peptide LL-37, to determine how this evolved trait affects its interaction with biological membranes and how it influences its biological activities.

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