Abstract:
"The process of protein misfolding and aggregation has been a prime subject of research.
This process is identified in the main pathological event involved in several diseases like
Alzheimer’s disease (AD), Parkinson disease (PD), Huntington disease (HD), Type II
diabetes (T2D) and prion-related disorders among others.1-3 AD is the most prevalent
form of neurodegenerative diseases causing progressive attrition of cognition, task
performance ability, mood, speech, behaviour and memory.4,5,6 A recent report from the
National Center for Health Statistics (NCHS), USA suggests that deaths caused by
diseases like ischemic heart disease, brain stroke, AIDS (acquired immune deficiency
syndrome) and cancer have decreased significantly, while deaths caused by AD is on a
constant rise.7 Alarmingly, in the next decade AD is likely to become particularly
devastating for the poor and developing countries, severely affecting their public health
and economy.8 For this reason, both scientific and clinical research community is putting
tremendous efforts into understanding the disease to develop molecular tools for early
diagnosis and cure. AD involves two major types of misfolded protein aggregates:
intracellular aggregates of the microtubule-associated tau protein (called neurofibrillary
tangles - NFT) and extracellular peptide aggregates known as senile plaques, mainly
composed of amyloid (Aβ) peptides.9 Aβ peptides are transmembrane peptides
produced by incorrect processing of the integral membrane protein called amyloid
precursor protein (APP).10 The physiological function of Aβ peptide in normal brain is
not completely understood, although it is said to be playing a vital role in neurogenesis
and modulation of synaptic plasticity.11"
