Gladstone Christopher Jayakumar

Preparation and antimicrobial activity of scleraldehyde from Schizophyllum commune.

The present study investigates the antimicrobial activity of oxidized schizophyllan (scleraldehyde) against Gram-positive and Gram-negative bacteria by diffusion and tube dilution analysis. Schizophyllan is a natural polysaccharide produced by fungi of the genus Schizophyllum. Periodate oxidation specifically cleaves the vicinal glycols in scleraldehyde to form their dialdehyde derivatives. The antibacterial activity exhibited by scleraldehyde was defined using various tests such as the disc diffusion assay, minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC). MIC and MBC values were found to be in the range of 3.0-8.0 mg/mL. Hence, the present studies establish that the scleraldehyde possesses effective antibacterial properties and can be used as a biopreservative for preservation of raw hides and skins.

A microscopic evaluation of collagen-bilirubin interactions: in vitro surface phenomenon.

This study is carried out to understand the morphology variations of collagen I matrices influenced by bilirubin. The characteristics of bilirubin interaction with collagen ascertained using various techniques like XRD, CLSM, fluorescence, SEM and AFM. These techniques are used to understand the distribution, expression and colocalization patterns of collagen–bilirubin complexes. The present investigation mimic the in vivo mechanisms created during the disorder condition like jaundice. Fluorescence technique elucidates the crucial role played by bilirubin deposition and interaction during collagen organization. Influence of bilirubin during collagen fibrillogenesis and banding patterns are clearly visualize using SEM. As a result, collagen–bilirubin complex provides different reconstructed patterns because of the influence of bilirubin concentration. Selectivity, specificity and spatial organization of collagen–bilirubin are determined through AFM imaging. Consequently, it is observed that the morphology and quantity of the bilirubin binding to collagen varied by the concentrations and the adsorption rate in protein solutions. Microscopic studies of collagen–bilirubin interaction confirms that bilirubin influence the fibrillogenesis and alter the rate of collagen organization depending on the bilirubin concentration. This knowledge helps to develop a novel drug to inhibit the interface point of interaction between collagen and bilirubin.

Molecular Understanding of Collagen Stabilization: Interaction of Valeraldehyde with Collagen

The present study explains the molecular level interaction of valeraldehyde with collagen. Valeraldehyde is a monoaldehyde, which involves crosslinking with protein through covalent linkages. The role of valeraldehyde as a crosslinking agent for collagen stabilization was studied. Molecular modeling approaches was used to understand the interaction of collagen like peptide with valeraldehyde, which mimic the aldehyde tanning processes involved in protein stabilization. Crosslinking efficiency of valeraldehyde was found to increase with an increase in concentration due to the higher availability of aldehydic groups involved in crosslinking with collagen. Valeraldehyde interacted collagen membrane showed an increase in thermal stability by 25°C at pH 8. In the presence of valeraldehyde, collagen fibrils nucleation center was shifted from a lower to a higher range. Shift in the nucleation center was observed in the reduction of gelling time. Water accessibility in valeraldehyde interacted collagen membrane was reduced due to a higher crosslinking rate in the collagen. Modified collagen membrane by valeraldehyde at incubation of about 96 h showed higher resistance to collagenolytic activity of 81%. The amino groups reacting appear to be involved in crosslinking with valeraldehyde. Several interaction sites were identified and the docking energy obtained was −5.539 kcal/mol. The participation of the aldehyde group with amino groups in collagen was observed, which plays a dominant role in the stabilization of peptide by valeraldehyde. It was found that complexes exhibit covalent bonding, hydrogen bonding and electrostatic interaction in the process of stabilization.