Ignacio (Nacho) Asial Email & Phone Number

DotBio is an early-stage Biopharma company specialized in next-generation domain antibody therapies, with a particular focus in immuno-oncology.

Undergraduate course: Discovery and Development of Therapeutic AntibodiesGraduate course: Research and Development of Modern Biopharmaceuticals

San Francisco

Collaboration with Nanyang Technological University, Singapore.

Development of engineered antibodies for niche therapeutic applications.

Further development of projects started during my PhD.

"NOVEL METHODS AND SCREENS FOR PROTEIN STABILITY ENGINEERING"Supervisors: Prof. Pär Nordlund and Dr. Tobias Cornvik.- Development of a colony-based, activity-independent biophysical screen for the identification of protein mutants with improved thermal stability inside the cell:A new thermostability screen was developed, named Hot Colony Fitlration (Hot-CoFi), which has the advantage of being activity-independent and therefore universally applicable to any target which can… Show more "NOVEL METHODS AND SCREENS FOR PROTEIN STABILITY ENGINEERING"Supervisors: Prof. Pär Nordlund and Dr. Tobias Cornvik.- Development of a colony-based, activity-independent biophysical screen for the identification of protein mutants with improved thermal stability inside the cell:A new thermostability screen was developed, named Hot Colony Fitlration (Hot-CoFi), which has the advantage of being activity-independent and therefore universally applicable to any target which can be expressed in a colony-forming micro-organism. Random mutagenesis libraries were created for 12 diverse targets representing different potential applications for the method. These libraries were screened by Hot-CoFi, identifying stable variants with stability improvements ranging between 5ᵒC and 26ᵒC. Publication: Asial I. et al. Nature Communications. 2013, 4:2901.- Creation of a phage display library based on the 10th Fibronectin type III (10FN3) domain:A new phagemid vector was created, allowing for the display of 10FN3 domain as a fusion with g3p coat protein. A phage display library was created by Kunkel mutagenesis. Two loops were randomized (BC and FG loops) using skewed oligonucleotides leading to a bias for Tyr, Ser and Gly residues, obtaining a functional diversity of 4 x10^10 unique members. The library was panned against 5 diverse targets, identifying binders against 4 of them, with affinities ranging between 1-10μM.- Development of a new methods for the identification of protein-protein interactions inside the cell:The Hot-CoFi method was modified to allow for the identification of protein stabilization through the interaction with a partner.Techniques employed: molecular biology, directed-evolution, phage display, protein expression and purification, surface plasmon resonance, biolayer interferometry, X-ray crystallography, differential scanning fluorimetry, differential static light scattering. Show less

- Cloning, production and purification of DNA-binding domains.- Protein stability characterization by Thermofluor.

Doctor Of Philosophy - Phd, Biochemistry, Biophysics And Molecular Biology

M.Sc., Protein Engineering, Structural Biochemistry, Molecular Modelling

M.Sc., Health-Applied Biotechnology