Reach Us +447897072958
All submissions of the EM system will be redirected to Online Manuscript Submission System. Authors are requested to submit articles directly to Online Manuscript Submission System of respective journal

Mini Review - (2023) Volume 12, Issue 5

Protein Folding and Misfolding: Implications for Disease

Pan Annabelle*
*Correspondence: Pan Annabelle, Department of Biochemistry, Jagiellonian University Medical College, Kopernika 7b st. Kraków 31-034, Poland, Email:
Department of Biochemistry, Jagiellonian University Medical College, Kopernika 7b st. Kraków 31-034, Poland

Received: 01-Sep-2023, Manuscript No. IJDRT-23-118233; Editor assigned: 02-Sep-2023, Pre QC No. P-118233; Reviewed: 15-Sep-2023, QC No. Q-118233; Revised: 22-Sep-2023, Manuscript No. R-118233; Published: 29-Sep-2023, DOI: 10.37421/2277-1506.2023.12.418


The folding of proteins is a fundamental process in biology, essential for their structure and function. However, this intricate ballet can sometimes go awry, leading to protein misfolding, a phenomenon closely associated with various diseases. In this article, we explore the mechanics of protein folding, the consequences of misfolding, and the critical role it plays in ailments like Alzheimer's, Parkinson's, and prion diseases. Understanding the intricacies of protein folding and misfolding is central to unraveling the mysteries of these devastating conditions and holds the key to potential therapeutic interventions. S6t3Bh9Gwo


Various • Protein • Misfolding


Proteins, the workhorses of life, are intricate molecules with complex three-dimensional structures. The manner in which a protein folds into its final shape is critical to its functionality. The process of protein folding is highly precise and, under normal conditions, results in a functional and biologically active molecule.

Literature Review

Protein folding is orchestrated by a combination of chemical and physical forces, including hydrogen bonds, hydrophobic interactions, van der Waals forces, and electrostatic interactions. The primary structure, or sequence of amino acids, dictates the intricate folding pattern, culminating in the formation of a specific three-dimensional structure. Protein misfolding occurs when a protein adopts an incorrect, non-functional structure. This misfolding can result from genetic mutations, environmental factors, or the natural aging process. When misfolded proteins accumulate, they can disrupt cellular function and give rise to diseases. For instance, in Alzheimer's and Parkinson's diseases, misfolded proteins aggregate, forming toxic clumps that damage neurons and lead to cognitive and motor deficits [1,2].


Alzheimer's disease is characterized by the accumulation of misfolded beta-amyloid and tau proteins. These proteins form amyloid plaques and neurofibrillary tangles, which are hallmark pathological features of the disease. The precise mechanism of protein misfolding in Alzheimer's remains a subject of intense research. In Parkinson's disease, misfolding of the alphasynuclein protein leads to the formation of lewy bodies in neurons. These protein aggregates impair cellular function and result in the motor symptoms associated with the disease. Prion diseases, like Creutzfeldt-Jakob disease and mad cow disease, involve the transmission of misfolded proteins from one individual to another. These abnormal proteins induce the misfolding of normal proteins, creating a cascade effect that leads to severe neurological degeneration [3,4].

Prion diseases, also known as transmissible spongiform encephalopathies represent a group of rare and fatal neurodegenerative disorders that have intrigued and baffled scientists for decades. These enigmatic diseases are characterized by the accumulation of abnormal prion proteins in the brain, leading to severe neurological dysfunction. This article delves into the fascinating world of prion diseases, exploring their origins, mechanisms, and the profound implications they have for biology and medicine. Prions are not your typical infectious agents. Unlike bacteria, viruses, or fungi, prions are solely composed of protein. These misfolded proteins have the astonishing capacity to induce the misfolding of their normal counterparts, converting them into abnormal prions, setting off a chain reaction. Understanding protein misfolding has profound implications for the development of therapies for these devastating diseases. Researchers are exploring various strategies to prevent, slow, or reverse the misfolding process, including the use of small molecules, antibodies, and gene therapies [5,6].


The study of protein folding and misfolding has unveiled a new frontier in biomedical research. It highlights the pivotal role that misfolded proteins play in the onset and progression of several debilitating diseases. By gaining a deeper understanding of the intricacies of protein folding and misfolding, researchers and clinicians are moving closer to innovative therapeutic strategies that may one day offer hope to those affected by these conditions. The journey to unlock the secrets of protein misfolding is ongoing, and its implications for disease prevention and treatment are profound



Conflict of Interest

No potential conflict of interest was reported by the authors.


  1. Rabin, Nira, Yue Zheng, Clement Opoku-Temeng and Yixuan Du, et al. "Biofilm formation mechanisms and targets for developing antibiofilm agents." Future Med Chem 7 (2015): 493-512.

    Google Scholar, Crossref, Indexed at

  2. Kaiser, Pia, Jana Wächter and Maike Windbergs. "Therapy of infected wounds: Overcoming clinical challenges by advanced drug delivery systems."Drug Deliv Transl Res11 (2021): 1545-1567.

    Google Scholar, Crossref, Indexed at

  3. Martin, Claire, Wan LiLow, Abhishek Gupta and Mohd Cairul Iqbal Mohd Amin, et al. "Strategies for antimicrobial drug delivery to biofilm."Curr Pharm Des 21 (2015): 43-66.
  4. Janakiraman, Vijay, Derek Englert, Arul Jayaraman and Harihara Baskaran. "Modeling growth and quorum sensing in biofilms grown in microfluidic chambers" Ann Biomed Eng 37 (2009): 1206-1216.

    Google Scholar, Crossref

  5. Sou, Tomás, Irena Kukavica-Ibrulj, Fadi Soukarieh and Nigel Halliday, et al. "Model-based drug development in pulmonary delivery: Pharmacokinetic analysis of novel drug candidates for treatment of Pseudomonas aeruginosa lung infection."J Pharm Sci 108 (2019): 630-640.

    Google Scholar, Crossref, Indexed at

  6. Mannermaa, Eliisa, Kati-Sisko Vellonen and Arto Urtti. "Drug transport in corneal epithelium and blood–retina barrier: Emerging role of transporters in ocular pharmacokinetics."Adv Drug Deliv Rev58 (2006): 1136-1163.

    Google Scholar, Crossref, Indexed at