title: Role of PAMAM-OH dendrimers against the fibrillation pathway of biomolecules.
abstract: The binding behavior of nanoparticle with proteins determines its biocompatibility. This study reports the interaction of ten different biomolecules (proteins-BSA, HSA, haemoglobin, gamma globulin, transferrin and enzymes-hog and bacillus amylase, lysozyme from chicken and human and laccases from Tramates versicolor) with a surface group hydroxylated Poly AMido AMide dendrimer (PAMAM) of generation 5. The study has utilized various spectroscopic methods like UV-vis spectroscopy, Fluorescence emission, Synchronous, 3-D spectroscopy and Circular Dichroism to detect the binding induced structural changes in biomolecules that occur upon interaction with mounting concentration of the dendrimers. Aggregation of proteins results in the formation of amyloid fibrils causing several human diseases. In this study, fibrillar samples of all ten biomolecules formed in the absence and the presence of dendrimers were investigated with Congo Red absorbance and ThT Assay to detect fibril formation, Trp Emission and 3-D scan to evaluate the effect of fibrillation on aromatic environment of biomolecules, and CD spectroscopy to measure the conformational changes in a quantitative manner. These assays have generated useful information on the role of dendrimers in amyloid fibril formation of biomolecules. The outcomes of the study remain valuable in evaluating the biological safety of PAMAM-OH dendrimers for their biomedical application in vivo.
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Gajalakshmi
authors.initials: G
authors.lastname: Sekar
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Ida
authors.initials: I
authors.lastname: Florance
authors.affiliation: School of Advanced Sciences, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: A
authors.initials: A
authors.lastname: Sivakumar
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore 632014, Tamil Nadu, India.
authors.forename: Amitava
authors.initials: A
authors.lastname: Mukherjee
authors.affiliation: Centre for Nanobiotechnology, VIT University, Vellore 632014, Tamil Nadu, India. Electronic address: nchandra40@hotmail.com.
authors.forename: Natarajan
authors.initials: N
authors.lastname: Chandrasekaran
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D030161:Avian Proteins / Q000737:chemistry; D001412:Bacillus subtilis / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry; D001487:Basidiomycota / Q000201:enzymology; D002417:Cattle; D002645:Chickens; D050091:Dendrimers / Q000737:chemistry*; D000431:Ethanol / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry; D006801:Humans; D042845:Laccase / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry; D066329:Protein Aggregates; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry; D013552:Swine; D014168:Transferrin / Q000737:chemistry; D000516:alpha-Amylases / Q000737:chemistry; D005719:gamma-Globulins / Q000737:chemistry
chemical_list: D000682:Amyloid; D030161:Avian Proteins; D001426:Bacterial Proteins; D050091:Dendrimers; D005656:Fungal Proteins; C104700:PAMAM Starburst; D066329:Protein Aggregates; D012709:Serum Albumin; D014168:Transferrin; D005719:gamma-Globulins; D000431:Ethanol; D042845:Laccase; D000516:alpha-Amylases; D009113:Muramidase
keywords: Biomolecules; Dendrimers; Interaction