| 1. |
- Bose, Partha Pratim, et al.
(författare)
-
Effects of Congo Red on A beta(1-40) Fibril Formation Process and Morphology
- 2010
-
Ingår i: ACS CHEMICAL NEUROSCIENCE. - : American Chemical Society (ACS). - 1948-7193. ; 1:4, s. 315-324
-
Tidskriftsartikel (refereegranskat)abstract
- Alzheimer's disease (AD), an age-related neurodegenerative disorder, is the most common form of dementia, and the seventh-leading cause of death in the United States. Current treatments offer only symptomatic relief; thus, there is a great need for new treatments with disease-modifying potential. One pathological hallmark of AD is so-called senile plaques, mainly made up of beta-sheet-rich assemblies of 40- or 42-residue amyloid beta-peptides (A beta). Hence, inhibition of A beta aggregation is actively explored as an option to prevent or treat AD. Congo red (CR) has been widely used as a model antiamyloid agent to prevent A beta aggregation. Herein, we report detailed morphological studies on the effect of CR as an antiamyloid agent, by circular dichroism spectroscopy, photo-induced cross-linking reactions, and atomic force microscopy. We also demonstrate the effect of CR on a preaggregated sample of A beta(1-40). Our result suggests that A beta(1-40) follows a different path for aggregation in the presence of CR.
|
|
| 2. |
- Bose, Partha Pratim, et al.
(författare)
-
In vitro ADMET and physicochemical investigations of poly-N-methylated peptides designed to inhibit Aβ aggregation
- 2010
-
Ingår i: Bioorganic & Medicinal Chemistry. - : Elsevier BV. - 0968-0896 .- 1464-3391. ; 18:16, s. 5896-5902
-
Tidskriftsartikel (refereegranskat)abstract
- N-Methylation is a common strategy for improving oral bioavailability of peptide-based lead structures. Herein, we present a detailed study on how the degree of N-methylation affects the absorption-distribution-metabolism-excretion-toxicity (ADMET) properties such as solubility, membrane transport, proteolytic stability, and general cell toxicity of the investigated peptides. As representative structures we chose hexapeptides 1-8. These peptides, corresponding to N-methylated analogues of residues 16-21 and 32-37 of the Abeta-peptide, pathological hallmark of Alzheimer's disease (AD), have previously been shown to inhibit aggregation of Abeta fibrils in vitro. This study suggests that poly-N-methylated peptides are non-toxic and have enhanced proteolytic stability over their non-methylated analogues. Furthermore, solubility in aqueous solution is seen to increase with increased degree of N-methylation, while membrane transport was found to be low for all investigated hexapeptides. The present results, together with those reported in the literature, suggest that poly-N-methylated peptides, especially shorter or equal to six residues, can be suitable candidates for drug design.
|
|
| 3. |
- Bose, Partha Pratim, et al.
(författare)
-
Template-directed nucleation and growth of CdS nanocrystal : the role of helical and nonhelical nanofibers on their shape and size
- 2010
-
Ingår i: Journal of nanoparticle research. - : Springer Science and Business Media LLC. - 1388-0764 .- 1572-896X. ; 12:3, s. 713-718
-
Tidskriftsartikel (refereegranskat)abstract
- This study describes the use of chiral nature of synthetic self-assembled nanofibers for nucleation and growth of Cadmium sulfide (CdS) nanocrystals with different sizes and shapes in room temperature. The templates are built by immobilizing a peptide capping agent on the surface of synthetic self-assembled helical or nonhelical nanofibers and CdS nanocrystals were allowed to grow on them. It is observed that there are differences in shapes and sizes of the nanocrystals depending on the chiral nature of the nanofibers on which they were growing. Even the CdS nanocrystals grown on different chiral and achiral nanofibers differ markedly in their photoluminescence properties. Thus, here we introduce a new way of using chirality of nanofibers to nucleate and grow CdS nanocrystals of different shape, size, and optical property.
|
|
