Prasad, A. K., Martin, L. L., & Panwar, A. S. (2023). Helical intermediate formation and its role in amyloids of an amphibian antimicrobial peptide. Physical Chemistry Chemical Physics, 25(17), 12134-12147. (Link)
Prasad, A. K., Tiwari, C., Ray, S., Holden, S., Armstrong, D. A., Rosengren, K. J., ... & Martin, L. L. (2022). Secondary structure transitions for a family of amyloidogenic, antimicrobial uperin 3 peptides in contact with sodium dodecyl sulfate. ChemPlusChem, 87(1), e202100408. (Link)
Ray, S., Holden, S., Prasad, A. K., Martin, L. L., & Panwar, A. S. (2020). Exploring the role of peptide helical stability in the propensity of uperin 3.x peptides toward beta-aggregation. The Journal of Physical Chemistry B, 124(51), 11659-11670. (Link)
Prasad, A. K., Samajdar, R., Panwar, A. S., & Martin, L. L. (2023). The origin of secondary structure transitions and peptide self-assembly propensity in trifluoroethanol-water mixtures. bioRxiv, 2023-09. (Communicated in Physical Chemistry Chemical Physics). (Link)
Prasad, A. K., Martin, L. L., & Panwar, A. S. Roles of mutation and concentration in peptide aggregation of U3.x antimicrobial peptides. (Under preparation, 75%)
Prasad, A. K., Martin, L. L., Panwar, A. S., & Arumugam, S. Rational design of amyloidogenic antimicrobial peptides using BiGAN deep learning model. (Under preparation)
Conferences
Lorne Proteins 2023 Lorne, VIC, Australia
RACI 2022 National Congress Brisbane, Australia
Computer-Aided Drug Design and Protein Analysis, 2021 IIT Varanasi, India
BioSungam 2018 NIT, Prayagraj, India