## 1 Introduction  
Alzheimer's disease (AD) is a sporadic and hereditary neurodegenerative illness, which causes ammestic cognitive impairment in its archetypal form and non-amnestic cognitive impairment in its less prevalent variations [1]. Furthermore, neural atrophy and disrupted inter-neuronal connections can occur [2]. By 2050, it is thought that up to 107 million people will be affected throughout the world [3]. Furthermore, AD has become incurable and life-threatening and imposes a significant socioeconomic cost due to its multifactorial nature [4]. The biological and environmental underpinnings of AD, particularly its correlation with amyloid- and Tau-protein-related systems, have been revealed recently through the research of this topic. This paradigm is applicable to autosomal dominant AD but not to sporadic AD [5]. However, the precise molecular events and biological pathways underlying the disease have yet to be discovered [6]. One of the most difficult tasks in AD research is to assemble the vast framework of scientific evidence regarding the disorder, much of which appears to be contradictory, into a coherent and credible pathogenic process [7]. Within this context, therapeutic efforts are still trying to uncover targets that can significantly alter the clinical course of people with [PERSON]'s disease [1]. Among existing theories that characterize the development and evolution of AD, the amyloid hypothesis has been a long-term adherent to AD due to the involvement of various types of amyloid-beta peptides (A\(\beta\)) in the impairment of neuronal and cognitive function [4]. Emerge of extracellular-amyloid accumulation in the form of neuritic plaques and intracellular accumulation of hyperphosphorylated tau in the type of neurofibrillary tangle continues to be the main neuropathologic criterion for the diagnosis of AD [8]. Moreover, a recent study showed that the extensive collaborative linkages between A\(\beta\) and innate immunity's established anti/pro-inflammatory cytokines allow amyloid misfolding to be included in the growing immunopathic disease mechanism theories of AD [9]. In this scenario, Alzheimer's symptoms develop, and the individuals show significant cognitive impairments [10]. Many researchers have refocused on finding a distinct molecular assembly of defined size, which describes the key cause of AD after the amyloid cascade hypothesis was reformulated. The main focus of this hypothesis was related to oligomeric aggregates of A\(\beta\) as the primary toxic species causing AD [11; 12]. It was also showed that the A\(\beta\) oligomers have noxious effects on post-synaptic protein Neuroligin-1 (NLGN1), which has critical roles in synapse formation, maturation, plasticity and maintenance [13]. The most common forms of A\(\beta\) in the human brain were proved to be A\(\beta_{(1-40)}\) and A\(\beta_{(142)}\). However, the A\(\beta_{(25-35)}\) fragment, which is physiologically predominant in aged individuals, has just been revealed to play a key role in AD due to its particular aggregation characteristics [14; 15]. Furthermore, it was noticed that there is a clear connection between the development of amyloid fibrils and the decrease in the native state's conformational stability of these peptides. The A\(\beta\) peptides in AD are inherently unfolded. Hence, a fibrillar aggregate with a rich \(\beta\)-sheet structure was identified in [PERSON]'s disease deposits [16; 17]. Despite a large number of studies, the underlying mechanisms that cause the A\(\beta\) aggregates to break the \(\beta\)-sheet structure remain unknown [18]. Therefore, the eradication of the A\(\beta\) peptide aggregates that form amyloid fibrils remains a complex task in the development of an anti-AD therapeutic strategy. Drug discovery efforts in [PERSON]'s disease face a unique set of hurdles [19]. Currently, altered biochemistry of the A\(\beta\) cycle is thought to be a major biological characteristic of AD and a possible therapy target [20].