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Fernando Bergasa-Caceres
Department of Chemistry, Princeton University, Princeton, NJ 08544, USA

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Short Biography

Fernando Bergasa-Caceres obtained a B.S. in Biochemistry and Molecular Biology at the Universidad Autonoma de Madrid (UAM) in 1990. While at the UAM he did research in scanning probe microscopy of proteins under the supervision of Prof. Juan J. Saenz. After spending 1991 at Tufts University studying protein folding with Prof. David L. Weaver, he joined Prof. Herschel A. Rabitz’s lab at Princeton in 1992, receiving his Ph.D. in Chemistry from Princeton University in 1996. In collaboration with Herschel A. Rabitz, Fernando Bergasa-Caceres has continued to publish in the field of protein folding. He serves on the Alumni Advisory Board and the Advisory Board at the Instituto de Fisica de la Materia Condensada, both at the UAM. Fernando Bergasa-Caceres is currently the Chairman and CEO of Redexis in Spain.

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Journal article
Published: 24 August 2021 in COVID
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In recent work, we proposed that effective therapeutic drugs aimed at treating the SARS-CoV-2 infection could be developed based on interdicting in the early steps of the folding pathway of key viral proteins, including the receptor binding domain (RBD) of the spike protein. In order to provide for a drug target on the protein, the earliest contact-formation event along the dominant folding pathway of the RBD spike protein was predicted employing the Sequential Collapse Model (SCM). The segments involved in the predicted earliest contact were suggested to provide optimal folding interdiction target regions (FITRs) for potential therapeutic drugs, with a focus on folding interdicting peptides (FIPs). In this paper, we extend our analysis to include 13 known single mutations of the RBD spike protein as well as the triple mutation B1.351 and the recent double mutation B1.617.2. The results show that the location of the FITR does not change in any of the 15 studied mutations, providing for a mutation-resistant drug design strategy for the RBD-spike protein.

ACS Style

Fernando Bergasa-Caceres; Herschel A. Rabitz. The Promise of Mutation Resistant Drugs for SARS-CoV-2 That Interdict in the Folding of the Spike Protein Receptor Binding Domain. COVID 2021, 1, 288 -302.

AMA Style

Fernando Bergasa-Caceres, Herschel A. Rabitz. The Promise of Mutation Resistant Drugs for SARS-CoV-2 That Interdict in the Folding of the Spike Protein Receptor Binding Domain. COVID. 2021; 1 (1):288-302.

Chicago/Turabian Style

Fernando Bergasa-Caceres; Herschel A. Rabitz. 2021. "The Promise of Mutation Resistant Drugs for SARS-CoV-2 That Interdict in the Folding of the Spike Protein Receptor Binding Domain." COVID 1, no. 1: 288-302.

Journal article
Published: 10 August 2021 in International Journal of Molecular Sciences
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The initial steps of the folding pathway of the C-terminal domain of the murine prion protein mPrP(90–231) are predicted based on the sequential collapse model (SCM). A non-local dominant contact is found to form between the connecting region between helix 1 and β-sheet 1 and the C-terminal region of helix 3. This non-local contact nucleates the most populated molten globule-like intermediate along the folding pathway. A less stable early non-local contact between segments 120–124 and 179–183, located in the middle of helix 2, promotes the formation of a less populated molten globule-like intermediate. The formation of the dominant non-local contact constitutes an example of the postulated Nature’s Shortcut to the prion protein collapse into the native structure. The possible role of the less populated molten globule-like intermediate is explored as the potential initiation point for the folding for three pathogenic mutants (T182A, I214V, and Q211P in mouse prion numbering) of the prion protein.

ACS Style

Fernando Bergasa-Caceres; Herschel Rabitz. Identification of Two Early Folding Stage Prion Non-Local Contacts Suggested to Serve as Key Steps in Directing the Final Fold to Be Either Native or Pathogenic. International Journal of Molecular Sciences 2021, 22, 8619 .

AMA Style

Fernando Bergasa-Caceres, Herschel Rabitz. Identification of Two Early Folding Stage Prion Non-Local Contacts Suggested to Serve as Key Steps in Directing the Final Fold to Be Either Native or Pathogenic. International Journal of Molecular Sciences. 2021; 22 (16):8619.

Chicago/Turabian Style

Fernando Bergasa-Caceres; Herschel Rabitz. 2021. "Identification of Two Early Folding Stage Prion Non-Local Contacts Suggested to Serve as Key Steps in Directing the Final Fold to Be Either Native or Pathogenic." International Journal of Molecular Sciences 22, no. 16: 8619.

Journal article
Published: 29 September 2018 in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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In this paper, the Sequential Collapse Model (SCM) for protein folding pathways is applied to investigate the location of the non-local contacts in the intrinsically disordered state of α-synuclein, a protein implicated in the onset and spreading of several serious neurodegenerative diseases. The model relies on the entropic cost of forming protein loops due to self-crowding effects, and the protein sequence to determine contact location and stability. It is found that the model predicts the existence of several possible non-local contacts, and the location of the non-local contacts is consistent with existing experimental evidence. The bearing of these findings on the pathogenic mechanism and its regulation is discussed.

ACS Style

Fernando Bergasa-Caceres; Herschel A. Rabitz. Predicting the location of the non-local contacts in α-synuclein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2018, 1866, 1201 -1208.

AMA Style

Fernando Bergasa-Caceres, Herschel A. Rabitz. Predicting the location of the non-local contacts in α-synuclein. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2018; 1866 (12):1201-1208.

Chicago/Turabian Style

Fernando Bergasa-Caceres; Herschel A. Rabitz. 2018. "Predicting the location of the non-local contacts in α-synuclein." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1866, no. 12: 1201-1208.