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Palak Sharma,
Naisergik Deepika Khanna,
- Student, Department of Chemistry, N.S.C.B.M., Government College Hamirpur (H.P.), Himachal Pradesh, India
- Assistant Professor, Department of Chemistry, N.S.C.B.M., Government College Hamirpur (H.P.), Himachal Pradesh, India
Abstract
Research on protein misfolding has identified several important diseases in which abnormal protein structures play a major role. In Alzheimer’s disease, Amyloid-beta (Aβ) peptides and Tau proteins can misfold and accumulate. Prion diseases are unusual because a misfolded protein can act as a template and encourage other normal proteins to adopt an abnormal structure. Understanding the chemistry behind protein folding is therefore important not only for basic research but also for modern medicine. By studying the structure–activity relationships (SAR) of protein aggregates, researchers can develop molecules such as molecular tweezers and foldamers that may interfere with harmful aggregates while minimizing effects on healthy cells. As the global population ages, understanding and controlling protein misfolding is becoming increasingly important.
Keywords: Protein Misfolding Disease, Amyloid Beta, Chemical Biology, Amino Acids, Toxicity, Foldamers, Structure-Activity Relationship.
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International Journal of Biochemistry and Biomolecule Research
| Volume | 04 | |
| 02 | ||
| Received | 14/08/2026 | |
| Accepted | 23/09/2026 | |
| Published | 30/09/2026 | |
| Publication Time | 47 Days |