Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Using supramolecular hydrogels to discover the interactions between proteins and molecular nanofibers of small molecules.

ABSTRACT: Here we report the first example of the use of supramolecular hydrogels to discover the protein targets of aggregates of small molecules.

SUBMITTER: Gao Y

PROVIDER: S-EPMC3728678 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

Using supramolecular hydrogels to discover the interactions between proteins and molecular nanofibers of small molecules.

Gao Yuan Y Long Marcus J C MJ Shi Junfeng J Hedstrom Lizbeth L Xu Bing B

Chemical communications (Cambridge, England) 20120717 67

Here we report the first example of the use of supramolecular hydrogels to discover the protein targets of aggregates of small molecules. ...[more]

PMID: 22801479

Similar Datasets

Electrostatic interactions regulate the release of small molecules from supramolecular hydrogels.

Project description:Supramolecular hydrogels have great potential as biomaterials for sustained delivery of therapeutics. While peptide-based supramolecular hydrogels have been developed that show promise for drug delivery applications, the high cost of production has limited their widespread adoption. Low molecular weight (LMW) supramolecular hydrogels are emerging as attractive and inexpensive alternatives to peptide-based hydrogels. We recently reported novel cationic fluorenylmethyloxycarbonyl-modified phenylalanine (Fmoc-Phe) hydrogels for localized and sustained in vivo release of an anti-inflammatory agent for functional pain remediation. In an effort to further elucidate design principles to optimize these materials for delivery of a variety of molecular agents, we herein report a systematic examination of electrostatic effects on the release of cargo molecules from Fmoc-Phe derived hydrogels. Specifically, we interrogate the release of cationic, anionic, and neutral cargo molecules from a series of cationic and anionic Fmoc-Phe derived hydrogels. We observed that cargo was readily released from the hydrogels except when the cargo and hydrogel network had complementary charges, in which case the cargo was highly retained in the network. These results demonstrate that the electrostatic characteristics of both the hydrogel network and the specific cargo are critical design parameters in the formulation of LMW supramolecular hydrogel systems in the development of next-generation materials for drug delivery applications.

| S-EPMC7429908 | biostudies-literature

Supramolecular nanofibers and hydrogels of nucleopeptides.

Project description: Not available

| S-EPMC3251214 | biostudies-literature

Molecular nanofibers of olsalazine form supramolecular hydrogels for reductive release of an anti-inflammatory agent.

Project description:Conjugation of tripeptide derivatives with olsalazine, a clinically used anti-inflammatory prodrug, yields small molecules that self-assemble in water to form supramolecular hydrogels that undergo a gel-to-sol phase transition upon reduction, resulting in the controlled release of 5-aminosalicylic acid as the anti-inflammatory agent. This methodology will ultimately lead to new biomaterials for site-specific drug delivery.

| S-EPMC3238101 | biostudies-literature

Methods of probing the interactions between small molecules and disordered proteins.

Project description:It is generally recognized that a large fraction of the human proteome is made up of proteins that remain disordered in their native states. Despite the fact that such proteins play key biological roles and are involved in many major human diseases, they still represent challenging targets for drug discovery. A major bottleneck for the identification of compounds capable of interacting with these proteins and modulating their disease-promoting behaviour is the development of effective techniques to probe such interactions. The difficulties in carrying out binding measurements have resulted in a poor understanding of the mechanisms underlying these interactions. In order to facilitate further methodological advances, here we review the most commonly used techniques to probe three types of interactions involving small molecules: (1) those that disrupt functional interactions between disordered proteins; (2) those that inhibit the aberrant aggregation of disordered proteins, and (3) those that lead to binding disordered proteins in their monomeric states. In discussing these techniques, we also point out directions for future developments.

| S-EPMC5533867 | biostudies-other

Interactions between cellular proteins and morphologically different nanoscale aggregates of small molecules.

Project description:Depending on the methods of preparation, amphiphilic small molecules aggregate to form nanostructures with different morphologies that interact with cytosol proteins in a drastically different manner, thus illustrating the first example of morphological dependent protein binding of nanoscale molecular aggregates.

| S-EPMC3677794 | biostudies-literature

The conjugation of nonsteroidal anti-inflammatory drugs (NSAID) to small peptides for generating multifunctional supramolecular nanofibers/hydrogels.

Project description:Here we report supramolecular hydrogelators made of nonsteroidal anti-inflammatory drugs (NSAID) and small peptides. The covalent linkage of Phe-Phe and NSAIDs results in conjugates that self-assemble in water to form molecular nanofibers as the matrices of hydrogels. When the NSAID is naproxen (1), the resultant hydrogelator 1a forms a hydrogel at a critical concentration (cgc) of 0.2 wt % at pH 7.0. Hydrogelator 1a, also acting as a general motif, enables enzymatic hydrogelation in which the precursor turns into a hydrogelator upon hydrolysis catalyzed by a phosphatase at physiological conditions. The conjugates of Phe-Phe with other NSAIDs, such as (R)-flurbiprofen (2), racemic flurbiprofen (3), and racemic ibuprofen (4), are able to form molecular hydrogels, except in the case of aspirin (5). After the conjugation with the small peptides, NSAIDs exhibit improved selectivity to their targets. In addition, the peptides made of D-amino acids help preserve the activities of NSAIDs. Besides demonstrating that common NSAIDs are excellent candidates to promote aromatic-aromatic interaction in water to form hydrogels, this work contributes to the development of functional molecules that have dual or multiple roles and ultimately may lead to new molecular hydrogels of therapeutic agents for topical use.

| S-EPMC3678635 | biostudies-literature

Catalytic dephosphorylation of adenosine monophosphate (AMP) to form supramolecular nanofibers/hydrogels.

Project description:The use of enzyme to instruct the self-assembly of the nucleoside of adenosine in water provides a new class of molecular nanofibers/hydrogels as functional soft materials.

| S-EPMC3522864 | biostudies-literature

Ordered, adherent layers of nanofibers enabled by supramolecular interactions.

Project description:Aligned nanofibrous substrates can be created by electrospinning, but methods for creating multilamellar structures of aligned fibers are limited. Here, apposed nanofibrous scaffolds with pendant β-cyclodextrin (CD) were adhered together by adamantane (Ad) modified hyaluronic acid, exploiting the guest-host interactions of CD and Ad for macroscopic assembly. Stable user-defined multi-layered scaffolds were formed for cell culture or tissue engineering.

| S-EPMC4232958 | biostudies-literature

Reciprocal carbonyl-carbonyl interactions in small molecules and proteins.

Project description:Carbonyl-carbonyl n→π* interactions where a lone pair (n) of the oxygen atom of a carbonyl group is delocalized over the π* orbital of a nearby carbonyl group have attracted a lot of attention in recent years due to their ability to affect the 3D structure of small molecules, polyesters, peptides, and proteins. In this paper, we report the discovery of a "reciprocal" carbonyl-carbonyl interaction with substantial back and forth n→π* and π→π* electron delocalization between neighboring carbonyl groups. We have carried out experimental studies, analyses of crystallographic databases and theoretical calculations to show the presence of this interaction in both small molecules and proteins. In proteins, these interactions are primarily found in polyproline II (PPII) helices. As PPII are the most abundant secondary structures in unfolded proteins, we propose that these local interactions may have implications in protein folding.Carbonyl-carbonyl π* non covalent interactions affect the structure and stability of small molecules and proteins. Here, the authors carry out experimental studies, analyses of crystallographic databases and theoretical calculations to describe an additional type of carbonyl-carbonyl interaction.

| S-EPMC5517579 | biostudies-literature

Heterotypic Supramolecular Hydrogels Formed by Noncovalent Interactions in Inflammasomes.

Project description:The advance of structural biology has revealed numerous noncovalent interactions between peptide sequences in protein structures, but such information is less explored for developing peptide materials. Here we report the formation of heterotypic peptide hydrogels by the two binding motifs revealed by the structures of an inflammasome. Specifically, conjugating a self-assembling motif to the positively or negatively charged peptide sequence from the ASCPYD filaments of inflammasome produces the solutions of the peptides. The addition of the peptides of the oppositely charged and complementary peptides to the corresponding peptide solution produces the heterotypic hydrogels. Rheology measurement shows that ratios of the complementary peptides affect the viscoelasticity of the resulted hydrogel. Circular dichroism indicates that the addition of the complementary peptides results in electrostatic interactions that modulate self-assembly. Transmission electron microscopy reveals that the ratio of the complementary peptides controls the morphology of the heterotypic peptide assemblies. This work illustrates a rational, biomimetic approach that uses the structural information from the protein data base (PDB) for developing heterotypic peptide materials via self-assembly.

| S-EPMC7795891 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data