Biomedical subjects

Britto S Sandanaraj

Publications and source records attributed to Britto S Sandanaraj.

7 recordsLinked to original sources

PubMed2006

Tuning substrate selectivity of a cationic enzyme using cationic polymers.

Noncovalent interactions between an artificial molecular scaffold and a protein are interesting due to the possibility of reversible modulation of the activity of the protein. alpha-Chymotrypsin is a positively charged protein that has been shown to interact with negatively charged polymers. Here we show that positively charged polymers are also capable of electrostatically binding to this protein. The resulting experiments show that the ability of a polymer to bind a protein does not depend only on the pI of the protein. We also realized that the variations in charge density in the polymer backbone afford different selectivities of the enzyme toward charged substrates.

Cations↗

PubMed2006

Selective sensing of metalloproteins from nonselective binding using a fluorogenic amphiphilic polymer.

Nonconjugated fluorogenic amphiphilic polymers containing an anthracene chromophore exhibit fluorescence quenching in the presence of metalloproteins, although the binding of the polymer to proteins is not selective. The reason for this difference is that the possible conformational changes that protein binding could bring about on a polymer do not affect the fluorescence properties of a pendent chromophore in nonconjugated polymers. This is in contrast to the nonspecific binding and response found with conjugated polymers to proteins.

Fluorescent Dyes↗

PubMed2006

Comparison of facially amphiphilic biaryl dendrimers with classical amphiphilic ones using protein surface recognition as the tool.

Facially amphiphilic biaryl dendrimers are compared with the more classical benzyl ether amphiphilic dendrimers for molecular recognition, using protein binding as the probe. The protein used for the proposed study is chymotrypsin (ChT). A generation-dependent binding affinity was observed with the benzyl ether dendrimers, while the affinities were independent of generation in the case of the biaryl dendrimers. Similarly, although the ligands incorporated in both dendrons are the same, the biaryl dendrimers are able to bind more proteins compared to the benzyl ether dendrimers. For example, G3-dendron of biaryl dendrimer can bind six molecules of chymotrypsin, whereas G3-analogue of benzyl ether dendrimers can bind only three molecules of chymotrypsin. This result is consistent with our hypothesis that the internal layers of the facially amphiphilic biaryl dendrons are solvent-exposed and accessible for recognition. In addition, the systematic size differences in dendrons were also used to gain insights into the substrate selectivity that the enzyme gains upon binding to a ligand scaffold.

Dendrimers↗

PubMed2005

Noncovalent modification of chymotrypsin surface using an amphiphilic polymer scaffold: implications in modulating protein function.

We report here on a new amphiphilic homopolymer that binds noncovalently to proteins. This polymer not only binds to the target protein chymotrypsin with submicromolar affinity but also stabilizes the native structure of the protein. Since the polymer-protein binding process is based on electrostatic interaction, the bound protein can be released from the polymer surface and reactivated either by increasing the ionic strength or by adding complementary cationic surfactants. The electrostatic binding of polymer to the protein results in a marked change in the substrate specificity of chymotrypsin.

Animals↗

PubMed2005

Effect of guest molecule flexibility in access to dendritic interiors.

[structure: see text] Dendrimers are attractive scaffolds for catalysis, since catalytic sites can be isolated and the catalysts are recoverable and reusable. Herein, we show that conformationally constrained molecules have better access to dendritic cores compared to the more flexible counterparts. The results reported here should have implications in utilizing dendrimers as scaffolds for artificial selectivity in catalysis.

Catalysis↗

PubMed2004

Invertible amphiphilic homopolymers.

Stimuli-responsive polymers and assemblies are viable candidates for the so-called "smart" materials. In this communication, we report a new class of amphiphilic homopolymers that forms micelle-like structures in polar solvents and inverted micelle-like structures in apolar solvents. We demonstrate that these superstructures are the result of the changes in the molecular-level conformations in the monomer.

Acrylic Resins↗

PubMed2004

Sequences in dendrons and dendrimers.

Sequential incorporation of a variety of functional groups forms the basis for specificity in biomacromolecules. Introduction of such diversity and sequencing ability in artificial macromolecules is fundamentally interesting. In this paper, three different synthetic approaches have been used to build dendrons and dendrimers in which all the monomer units are different from each other. The synthetic strategies described in this paper involve the use of (i) an ABB(p) monomer, (ii) an ABB' monomer, and (iii) an ABB(m) monomer. The complementarity and the versatility of these synthetic approaches should render them useful for a variety of applications.

Biomimetic Materials↗