Intrinsic Amyloidogenic Behavior of Terminally Protected Amyloid β-peptide fragments: Aggregation and Amyloid-Like Fibril Formation

Suman, Saurav (2019) Intrinsic Amyloidogenic Behavior of Terminally Protected Amyloid β-peptide fragments: Aggregation and Amyloid-Like Fibril Formation. Masters thesis, Indian Institute of Science Education and Research Kolkata.

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Abstract

The present work represents the synthesis, characterization, conformational analysis, and aggregration studies in biological or physical domains. It shows the synthesis of diipeptides containing glycine, Lalanine and L-valine by solution phase methods, their characterization by NMR, FTIR and Mass spectroscopy, their morphological studies by Field Emission Scanning Electron Microscopy. The “Intrinsic Amyloidogenic Behavior of Terminally Protected Amyloid β-peptide fragment 29-30 and 39-40” represents synthesis of diipeptides containing glycine, Lalanine and L-valine by solution phase methods, their characterization by NMR, FTIR and Mass spectroscopy, their morphological studies by Field Emission Scanning Electron Microscopy. The dipeptides self-assembled to form amyloid-like fibrils. On the other hand, “Aib Modified Analogue of Amyloid β-Peptide Residue 37-38” represents the synthesis of the dipeptide containing glycine and -aminoisobutyric acid by solution phase methods, their characterization by NMR, FT-IR and Mass spectrometry. Morphological studies by Field Emission Scanning Electron Microscopy shows that the glycine containing peptide form amyloid-like fibrils. But the Aib analogue inhibits the fibril formation.

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