Biomaterial Database

Rottlerin dissolves pre-formed protein amyloid: a study on hen egg white lysozyme. 2011

Nandini Sarkar, and Manjeet Kumar, and Vikash Kumar Dubey

Department of Biotechnology, Indian Institute of Technology Guwahati, Assam, India.

BACKGROUND Deposition of protein fibrillar aggregates called amyloids in the tissue, is the principal cause of several degenerative diseases. Here, we have shown the disaggregation potential of rottlerin towards hen egg white lysozyme (HEWL) fibrils formed under alkaline conditions (pH-12.2). METHODS Several biophysical methods like Atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FTIR) and fluorescence emission spectra were used for the study. CONCLUSIONS Rottlerin exhibited instantaneous disaggregation effect on HEWL fibrils as monitored by Thioflavin T assay, anisotropy study and AFM imaging. Further we have monitored the conformational changes induced by rottlerin on the fibril in terms of surface hydrophobicity and secondary structure through 8-anilino-1-naphthalene sulfonic acid (ANS) fluorescence and FTIR study respectively. We have also attempted to elucidate the type of interaction between HEWL and rottlerin at pH-12.2 employing techniques like quenching study and FTIR. CONCLUSIONS Rottlerin seems to have potential application as anti-amyloid compound.

UI	MeSH Term	Description	Entries
D009113	Muramidase	A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.	Lysozyme,Leftose,N-Acetylmuramide Glycanhydrolase,Glycanhydrolase, N-Acetylmuramide,N Acetylmuramide Glycanhydrolase
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D000098	Acetophenones	Derivatives of the simplest aromatic ketone acetophenone (of general formula C6H5C(O)CH3).
D000682	Amyloid	A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease.	Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D001578	Benzopyrans	Compounds with a core of fused benzo-pyran rings.	Benzopyran,Chromene,Chromenes
D017550	Spectroscopy, Fourier Transform Infrared	A spectroscopic technique in which a range of wavelengths is presented simultaneously with an interferometer and the spectrum is mathematically derived from the pattern thus obtained.	FTIR,Fourier Transform Infrared Spectroscopy,Spectroscopy, Infrared, Fourier Transform
D057927	Hydrophobic and Hydrophilic Interactions	The thermodynamic interaction between a substance and WATER.	Hydrophilic Interactions,Hydrophilic and Hydrophobic Interactions,Hydrophilicity,Hydrophobic Interactions,Hydrophobicity,Hydrophilic Interaction,Hydrophilicities,Hydrophobic Interaction,Hydrophobicities,Interaction, Hydrophilic,Interaction, Hydrophobic,Interactions, Hydrophilic,Interactions, Hydrophobic
D058227	Amyloidogenic Proteins	Proteins that form the core of amyloid fibrils. For example, the core of amyloid A is formed from amyloid A protein, also known as serum amyloid A protein or SAA protein.	Amyloid Protein,Amyloidogenic Protein,Amyloid Proteins,Protein, Amyloid,Protein, Amyloidogenic,Proteins, Amyloid,Proteins, Amyloidogenic
D018625	Microscopy, Atomic Force	A type of scanning probe microscopy in which a probe systematically rides across the surface of a sample being scanned in a raster pattern. The vertical position is recorded as a spring attached to the probe rises and falls in response to peaks and valleys on the surface. These deflections produce a topographic map of the sample.	Atomic Force Microscopy,Force Microscopy,Scanning Force Microscopy,Atomic Force Microscopies,Force Microscopies,Force Microscopies, Scanning,Force Microscopy, Scanning,Microscopies, Atomic Force,Microscopies, Force,Microscopies, Scanning Force,Microscopy, Force,Microscopy, Scanning Force,Scanning Force Microscopies