A secondary structure within small peptides guiding spontaneous self-aggregation and nanoparticle formation
Year: 2024
Type: article
Abstract: baculovirus is a protein that self-aggregates forming a crystal structure known as polyhedra. Baculovirus occluded inside the crystal withstand for years at room temperature retaining infectivity. By investigating the smallest fragment from polyhedrin retaining the self-aggregation properties we identified a 29 amino acid sequence that spontaneously forms nanoparticles. This small sequence contains a β-sheet followed by an α-helix. We synthesized a variety of peptides with different amino acid sequences but similar secondary structure and discovered that the peptides self-aggregate forming nanoparticles of different geometries and sizes. Furthermore, peptides containing only the β-sheet or the α-helix aggregate also. This study led to the discovery of secondary structures that spontaneously self-aggregate forming nanoparticles even when fused to the green fluorescent protein.
Source: Nanoscale Advances
DOI: 10.1039/d4na00614c
Institution: Universidad Nacional Autónoma de México
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $1,962
Award: G1252727699
OpenAlex ID: W4404539820
