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Ordered Peptide Aggregation

Protein aggregation is inextricably involved with the etiology of several neurodegenerative diseases. This has stimulated widespread interest in understanding fundamental aspects involved with protein malfolding and events leading to a catastrophic aggregative phenomenon that causes age-dependent loss of cognitive functions. It is now believed that this process is initiated by ordered intermolecular interactions of polypeptide chains, further aided by other peripheral contacts, which stabilize prefibrillar intermediates eventually leading to amorphous and protease resistant proteinaceous aggregates. Examples of proteins related to neurodegenerative disorders include: beta-amyloid (Alzheimer's disease), prion (Mad cow disease), alpha-synuclein (Parkinson's disease), and huntingtin (Huntington's disease), to name a few.

However, a major lacuna in undertaking structural studies with such proteins stems from the amorphous nature of aggregated proteins, which prevents determination of detailed atomic structure by conventional diffraction methods, and highly insoluble nature of these aggregates further prohibits solution phase studies. In this context, it is desirable to develop small peptide constructs which are able to mimic structural aspects of large aggregating proteins for disease modeling and in-depth structural and morphological studies.

Dr. Sandeep Verma's research work at IIT-Kanpur is focused towards understanding potential role of conserved peptide motifs in aggregating proteins as focal points of agglomeration; development of nucleobase polymeric systems for biomimetic catalysis; and bone biomineralization. Recent published efforts from his group concern development of peptide constructs from the octarepeat region of prion proteins and also from a highly conserved V3 loop crown from HIV-1. Microscopic images of some fibrillar aggregates from his group are shown underneath.

More details about Dr. Verma's work, please visit his website:

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